data_9BXD
# 
_entry.id   9BXD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BXD         pdb_00009bxd 10.2210/pdb9bxd/pdb 
WWPDB D_1000284338 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXD 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marzena.pazgier@usuhs.edu 
_pdbx_contact_author.name_first         Marzena 
_pdbx_contact_author.name_last          Pazgier 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0594-5057 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Niu, L.'       1 ? 
'Tolbert, W.D.' 2 ? 
'Pazgier, M.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1961 
_citation.page_last                 1969 
_citation.title                     
'Optimization of a Piperidine CD4-Mimetic Scaffold Sensitizing HIV-1 Infected Cells to Antibody-Dependent Cellular Cytotoxicity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00403 
_citation.pdbx_database_id_PubMed   39563795 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, D.'                1  ?                   
primary 'Niu, L.'                2  ?                   
primary 'Ding, S.'               3  ?                   
primary 'Zhu, H.'                4  ?                   
primary 'Tolbert, W.D.'          5  ?                   
primary 'Medjahed, H.'           6  ?                   
primary 'Beaudoin-Bussieres, G.' 7  ?                   
primary 'Abrams, C.'             8  0000-0002-1240-0816 
primary 'Finzi, A.'              9  ?                   
primary 'Pazgier, M.'            10 ?                   
primary 'Smith 3rd, A.B.'        11 0000-0002-1712-8567 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'HIV-1 LM/HS clade A/E CRF01 gp120 core'                                                        39452.723 1   ? 
'H61Y, Q105H, V108I, H375S, N474D, I475M, K476R' ? ? 
2 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose                                                        221.208   9   ? 
?                                                ? ? 
3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'                                           238.305   1   ? 
?                                                ? ? 
4 non-polymer syn '(3S)-1-(4-L-arginylpiperazine-1-carbonyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' 525.019   1   ? 
?                                                ? ? 
5 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                                 118.174   1   ? 
?                                                ? ? 
6 water       nat water                                                                                           18.015    180 ? 
?                                                ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-acetamido-2-deoxy-beta-D-glucopyranose                                                        NAG   
3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'                                           EPE   
4 '(3S)-1-(4-L-arginylpiperazine-1-carbonyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' A1ATK 
5 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                                 MPD   
6 water                                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   PRO n 
1 3   VAL n 
1 4   TRP n 
1 5   LYS n 
1 6   ASP n 
1 7   ALA n 
1 8   ASP n 
1 9   THR n 
1 10  THR n 
1 11  LEU n 
1 12  PHE n 
1 13  CYS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  ALA n 
1 18  LYS n 
1 19  ALA n 
1 20  TYR n 
1 21  GLU n 
1 22  THR n 
1 23  GLU n 
1 24  VAL n 
1 25  HIS n 
1 26  ASN n 
1 27  VAL n 
1 28  TRP n 
1 29  ALA n 
1 30  THR n 
1 31  HIS n 
1 32  ALA n 
1 33  CYS n 
1 34  VAL n 
1 35  PRO n 
1 36  THR n 
1 37  ASP n 
1 38  PRO n 
1 39  ASN n 
1 40  PRO n 
1 41  GLN n 
1 42  GLU n 
1 43  ILE n 
1 44  HIS n 
1 45  LEU n 
1 46  GLU n 
1 47  ASN n 
1 48  VAL n 
1 49  THR n 
1 50  GLU n 
1 51  ASN n 
1 52  PHE n 
1 53  ASN n 
1 54  MET n 
1 55  TRP n 
1 56  LYS n 
1 57  ASN n 
1 58  ASN n 
1 59  MET n 
1 60  VAL n 
1 61  GLU n 
1 62  GLN n 
1 63  MET n 
1 64  HIS n 
1 65  GLU n 
1 66  ASP n 
1 67  ILE n 
1 68  ILE n 
1 69  SER n 
1 70  LEU n 
1 71  TRP n 
1 72  ASP n 
1 73  GLN n 
1 74  SER n 
1 75  LEU n 
1 76  GLN n 
1 77  PRO n 
1 78  CYS n 
1 79  VAL n 
1 80  LYS n 
1 81  LEU n 
1 82  THR n 
1 83  GLY n 
1 84  GLY n 
1 85  SER n 
1 86  VAL n 
1 87  ILE n 
1 88  LYS n 
1 89  GLN n 
1 90  ALA n 
1 91  CYS n 
1 92  PRO n 
1 93  LYS n 
1 94  ILE n 
1 95  SER n 
1 96  PHE n 
1 97  ASP n 
1 98  PRO n 
1 99  ILE n 
1 100 PRO n 
1 101 ILE n 
1 102 HIS n 
1 103 TYR n 
1 104 CYS n 
1 105 THR n 
1 106 PRO n 
1 107 ALA n 
1 108 GLY n 
1 109 TYR n 
1 110 VAL n 
1 111 ILE n 
1 112 LEU n 
1 113 LYS n 
1 114 CYS n 
1 115 ASN n 
1 116 ASP n 
1 117 LYS n 
1 118 ASN n 
1 119 PHE n 
1 120 ASN n 
1 121 GLY n 
1 122 THR n 
1 123 GLY n 
1 124 PRO n 
1 125 CYS n 
1 126 LYS n 
1 127 ASN n 
1 128 VAL n 
1 129 SER n 
1 130 SER n 
1 131 VAL n 
1 132 GLN n 
1 133 CYS n 
1 134 THR n 
1 135 HIS n 
1 136 GLY n 
1 137 ILE n 
1 138 LYS n 
1 139 PRO n 
1 140 VAL n 
1 141 VAL n 
1 142 SER n 
1 143 THR n 
1 144 GLN n 
1 145 LEU n 
1 146 LEU n 
1 147 LEU n 
1 148 ASN n 
1 149 GLY n 
1 150 SER n 
1 151 LEU n 
1 152 ALA n 
1 153 GLU n 
1 154 GLU n 
1 155 GLU n 
1 156 ILE n 
1 157 ILE n 
1 158 ILE n 
1 159 ARG n 
1 160 SER n 
1 161 GLU n 
1 162 ASN n 
1 163 LEU n 
1 164 THR n 
1 165 ASN n 
1 166 ASN n 
1 167 ALA n 
1 168 LYS n 
1 169 THR n 
1 170 ILE n 
1 171 ILE n 
1 172 VAL n 
1 173 HIS n 
1 174 LEU n 
1 175 ASN n 
1 176 LYS n 
1 177 SER n 
1 178 VAL n 
1 179 GLU n 
1 180 ILE n 
1 181 ASN n 
1 182 CYS n 
1 183 THR n 
1 184 ARG n 
1 185 PRO n 
1 186 SER n 
1 187 ASN n 
1 188 GLY n 
1 189 GLY n 
1 190 SER n 
1 191 GLY n 
1 192 SER n 
1 193 GLY n 
1 194 GLY n 
1 195 ASP n 
1 196 ILE n 
1 197 ARG n 
1 198 LYS n 
1 199 ALA n 
1 200 TYR n 
1 201 CYS n 
1 202 GLU n 
1 203 ILE n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 LYS n 
1 208 TRP n 
1 209 ASN n 
1 210 LYS n 
1 211 VAL n 
1 212 LEU n 
1 213 LYS n 
1 214 GLN n 
1 215 VAL n 
1 216 THR n 
1 217 GLU n 
1 218 LYS n 
1 219 LEU n 
1 220 LYS n 
1 221 GLU n 
1 222 HIS n 
1 223 PHE n 
1 224 ASN n 
1 225 ASN n 
1 226 LYS n 
1 227 THR n 
1 228 ILE n 
1 229 ILE n 
1 230 PHE n 
1 231 GLN n 
1 232 PRO n 
1 233 PRO n 
1 234 SER n 
1 235 GLY n 
1 236 GLY n 
1 237 ASP n 
1 238 LEU n 
1 239 GLU n 
1 240 ILE n 
1 241 THR n 
1 242 MET n 
1 243 HIS n 
1 244 SER n 
1 245 PHE n 
1 246 ASN n 
1 247 CYS n 
1 248 ARG n 
1 249 GLY n 
1 250 GLU n 
1 251 PHE n 
1 252 PHE n 
1 253 TYR n 
1 254 CYS n 
1 255 ASN n 
1 256 THR n 
1 257 THR n 
1 258 GLN n 
1 259 LEU n 
1 260 PHE n 
1 261 ASN n 
1 262 ASN n 
1 263 THR n 
1 264 CYS n 
1 265 ILE n 
1 266 GLY n 
1 267 ASN n 
1 268 GLU n 
1 269 THR n 
1 270 MET n 
1 271 LYS n 
1 272 GLY n 
1 273 CYS n 
1 274 ASN n 
1 275 GLY n 
1 276 THR n 
1 277 ILE n 
1 278 THR n 
1 279 LEU n 
1 280 PRO n 
1 281 CYS n 
1 282 LYS n 
1 283 ILE n 
1 284 LYS n 
1 285 GLN n 
1 286 ILE n 
1 287 ILE n 
1 288 ASN n 
1 289 MET n 
1 290 TRP n 
1 291 GLN n 
1 292 GLY n 
1 293 THR n 
1 294 GLY n 
1 295 GLN n 
1 296 ALA n 
1 297 MET n 
1 298 TYR n 
1 299 ALA n 
1 300 PRO n 
1 301 PRO n 
1 302 ILE n 
1 303 ASP n 
1 304 GLY n 
1 305 LYS n 
1 306 ILE n 
1 307 ASN n 
1 308 CYS n 
1 309 VAL n 
1 310 SER n 
1 311 ASN n 
1 312 ILE n 
1 313 THR n 
1 314 GLY n 
1 315 ILE n 
1 316 LEU n 
1 317 LEU n 
1 318 THR n 
1 319 ARG n 
1 320 ASP n 
1 321 GLY n 
1 322 GLY n 
1 323 ALA n 
1 324 ASN n 
1 325 ASN n 
1 326 THR n 
1 327 SER n 
1 328 ASN n 
1 329 GLU n 
1 330 THR n 
1 331 PHE n 
1 332 ARG n 
1 333 PRO n 
1 334 GLY n 
1 335 GLY n 
1 336 GLY n 
1 337 ASP n 
1 338 MET n 
1 339 ARG n 
1 340 ASP n 
1 341 ASN n 
1 342 TRP n 
1 343 ARG n 
1 344 SER n 
1 345 GLU n 
1 346 LEU n 
1 347 TYR n 
1 348 LYS n 
1 349 TYR n 
1 350 LYS n 
1 351 VAL n 
1 352 VAL n 
1 353 GLN n 
1 354 ILE n 
1 355 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   355 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HIV-1 Env' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Human immunodeficiency virus 1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11676 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            'HEK 293 GnT1-' 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ATK non-polymer                  . 
'(3S)-1-(4-L-arginylpiperazine-1-carbonyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' ? 'C23 H34 Cl F N8 O3' 525.019 
ALA   'L-peptide linking'          y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking'          y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking'          y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking'          y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking'          y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
EPE   non-polymer                  . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'     238.305 
GLN   'L-peptide linking'          y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking'          y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'            y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking'          y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer                  . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking'          y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking'          y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking'          y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking'          y METHIONINE ? 'C5 H11 N O2 S'      149.211 
MPD   non-polymer                  . '(4S)-2-METHYL-2,4-PENTANEDIOL' ? 'C6 H14 O2'          118.174 
NAG   'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'        221.208 
PHE   'L-peptide linking'          y PHENYLALANINE ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking'          y PROLINE ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking'          y SERINE ? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking'          y THREONINE ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking'          y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking'          y TYROSINE ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking'          y VALINE ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   VAL 1   42  ?   ?   ?   A . n 
A 1 2   PRO 2   43  ?   ?   ?   A . n 
A 1 3   VAL 3   44  44  VAL VAL A . n 
A 1 4   TRP 4   45  45  TRP TRP A . n 
A 1 5   LYS 5   46  46  LYS LYS A . n 
A 1 6   ASP 6   47  47  ASP ASP A . n 
A 1 7   ALA 7   48  48  ALA ALA A . n 
A 1 8   ASP 8   49  49  ASP ASP A . n 
A 1 9   THR 9   50  50  THR THR A . n 
A 1 10  THR 10  51  51  THR THR A . n 
A 1 11  LEU 11  52  52  LEU LEU A . n 
A 1 12  PHE 12  53  53  PHE PHE A . n 
A 1 13  CYS 13  54  54  CYS CYS A . n 
A 1 14  ALA 14  55  55  ALA ALA A . n 
A 1 15  SER 15  56  56  SER SER A . n 
A 1 16  ASP 16  57  57  ASP ASP A . n 
A 1 17  ALA 17  58  58  ALA ALA A . n 
A 1 18  LYS 18  59  59  LYS LYS A . n 
A 1 19  ALA 19  60  60  ALA ALA A . n 
A 1 20  TYR 20  61  61  TYR TYR A . n 
A 1 21  GLU 21  62  62  GLU GLU A . n 
A 1 22  THR 22  63  63  THR THR A . n 
A 1 23  GLU 23  64  64  GLU GLU A . n 
A 1 24  VAL 24  65  65  VAL VAL A . n 
A 1 25  HIS 25  66  66  HIS HIS A . n 
A 1 26  ASN 26  67  67  ASN ASN A . n 
A 1 27  VAL 27  68  68  VAL VAL A . n 
A 1 28  TRP 28  69  69  TRP TRP A . n 
A 1 29  ALA 29  70  70  ALA ALA A . n 
A 1 30  THR 30  71  71  THR THR A . n 
A 1 31  HIS 31  72  72  HIS HIS A . n 
A 1 32  ALA 32  73  73  ALA ALA A . n 
A 1 33  CYS 33  74  74  CYS CYS A . n 
A 1 34  VAL 34  75  75  VAL VAL A . n 
A 1 35  PRO 35  76  76  PRO PRO A . n 
A 1 36  THR 36  77  77  THR THR A . n 
A 1 37  ASP 37  78  78  ASP ASP A . n 
A 1 38  PRO 38  79  79  PRO PRO A . n 
A 1 39  ASN 39  80  80  ASN ASN A . n 
A 1 40  PRO 40  81  81  PRO PRO A . n 
A 1 41  GLN 41  82  82  GLN GLN A . n 
A 1 42  GLU 42  83  83  GLU GLU A . n 
A 1 43  ILE 43  84  84  ILE ILE A . n 
A 1 44  HIS 44  85  85  HIS HIS A . n 
A 1 45  LEU 45  86  86  LEU LEU A . n 
A 1 46  GLU 46  87  87  GLU GLU A . n 
A 1 47  ASN 47  88  88  ASN ASN A . n 
A 1 48  VAL 48  89  89  VAL VAL A . n 
A 1 49  THR 49  90  90  THR THR A . n 
A 1 50  GLU 50  91  91  GLU GLU A . n 
A 1 51  ASN 51  92  92  ASN ASN A . n 
A 1 52  PHE 52  93  93  PHE PHE A . n 
A 1 53  ASN 53  94  94  ASN ASN A . n 
A 1 54  MET 54  95  95  MET MET A . n 
A 1 55  TRP 55  96  96  TRP TRP A . n 
A 1 56  LYS 56  97  97  LYS LYS A . n 
A 1 57  ASN 57  98  98  ASN ASN A . n 
A 1 58  ASN 58  99  99  ASN ASN A . n 
A 1 59  MET 59  100 100 MET MET A . n 
A 1 60  VAL 60  101 101 VAL VAL A . n 
A 1 61  GLU 61  102 102 GLU GLU A . n 
A 1 62  GLN 62  103 103 GLN GLN A . n 
A 1 63  MET 63  104 104 MET MET A . n 
A 1 64  HIS 64  105 105 HIS HIS A . n 
A 1 65  GLU 65  106 106 GLU GLU A . n 
A 1 66  ASP 66  107 107 ASP ASP A . n 
A 1 67  ILE 67  108 108 ILE ILE A . n 
A 1 68  ILE 68  109 109 ILE ILE A . n 
A 1 69  SER 69  110 110 SER SER A . n 
A 1 70  LEU 70  111 111 LEU LEU A . n 
A 1 71  TRP 71  112 112 TRP TRP A . n 
A 1 72  ASP 72  113 113 ASP ASP A . n 
A 1 73  GLN 73  114 114 GLN GLN A . n 
A 1 74  SER 74  115 115 SER SER A . n 
A 1 75  LEU 75  116 116 LEU LEU A . n 
A 1 76  GLN 76  117 117 GLN GLN A . n 
A 1 77  PRO 77  118 118 PRO PRO A . n 
A 1 78  CYS 78  119 119 CYS CYS A . n 
A 1 79  VAL 79  120 120 VAL VAL A . n 
A 1 80  LYS 80  121 121 LYS LYS A . n 
A 1 81  LEU 81  122 122 LEU LEU A . n 
A 1 82  THR 82  123 123 THR THR A . n 
A 1 83  GLY 83  124 124 GLY GLY A . n 
A 1 84  GLY 84  198 198 GLY GLY A . n 
A 1 85  SER 85  199 199 SER SER A . n 
A 1 86  VAL 86  200 200 VAL VAL A . n 
A 1 87  ILE 87  201 201 ILE ILE A . n 
A 1 88  LYS 88  202 202 LYS LYS A . n 
A 1 89  GLN 89  203 203 GLN GLN A . n 
A 1 90  ALA 90  204 204 ALA ALA A . n 
A 1 91  CYS 91  205 205 CYS CYS A . n 
A 1 92  PRO 92  206 206 PRO PRO A . n 
A 1 93  LYS 93  207 207 LYS LYS A . n 
A 1 94  ILE 94  208 208 ILE ILE A . n 
A 1 95  SER 95  209 209 SER SER A . n 
A 1 96  PHE 96  210 210 PHE PHE A . n 
A 1 97  ASP 97  211 211 ASP ASP A . n 
A 1 98  PRO 98  212 212 PRO PRO A . n 
A 1 99  ILE 99  213 213 ILE ILE A . n 
A 1 100 PRO 100 214 214 PRO PRO A . n 
A 1 101 ILE 101 215 215 ILE ILE A . n 
A 1 102 HIS 102 216 216 HIS HIS A . n 
A 1 103 TYR 103 217 217 TYR TYR A . n 
A 1 104 CYS 104 218 218 CYS CYS A . n 
A 1 105 THR 105 219 219 THR THR A . n 
A 1 106 PRO 106 220 220 PRO PRO A . n 
A 1 107 ALA 107 221 221 ALA ALA A . n 
A 1 108 GLY 108 222 222 GLY GLY A . n 
A 1 109 TYR 109 223 223 TYR TYR A . n 
A 1 110 VAL 110 224 224 VAL VAL A . n 
A 1 111 ILE 111 225 225 ILE ILE A . n 
A 1 112 LEU 112 226 226 LEU LEU A . n 
A 1 113 LYS 113 227 227 LYS LYS A . n 
A 1 114 CYS 114 228 228 CYS CYS A . n 
A 1 115 ASN 115 229 229 ASN ASN A . n 
A 1 116 ASP 116 230 230 ASP ASP A . n 
A 1 117 LYS 117 231 231 LYS LYS A . n 
A 1 118 ASN 118 232 232 ASN ASN A . n 
A 1 119 PHE 119 233 233 PHE PHE A . n 
A 1 120 ASN 120 234 234 ASN ASN A . n 
A 1 121 GLY 121 235 235 GLY GLY A . n 
A 1 122 THR 122 236 236 THR THR A . n 
A 1 123 GLY 123 237 237 GLY GLY A . n 
A 1 124 PRO 124 238 238 PRO PRO A . n 
A 1 125 CYS 125 239 239 CYS CYS A . n 
A 1 126 LYS 126 240 240 LYS LYS A . n 
A 1 127 ASN 127 241 241 ASN ASN A . n 
A 1 128 VAL 128 242 242 VAL VAL A . n 
A 1 129 SER 129 243 243 SER SER A . n 
A 1 130 SER 130 244 244 SER SER A . n 
A 1 131 VAL 131 245 245 VAL VAL A . n 
A 1 132 GLN 132 246 246 GLN GLN A . n 
A 1 133 CYS 133 247 247 CYS CYS A . n 
A 1 134 THR 134 248 248 THR THR A . n 
A 1 135 HIS 135 249 249 HIS HIS A . n 
A 1 136 GLY 136 250 250 GLY GLY A . n 
A 1 137 ILE 137 251 251 ILE ILE A . n 
A 1 138 LYS 138 252 252 LYS LYS A . n 
A 1 139 PRO 139 253 253 PRO PRO A . n 
A 1 140 VAL 140 254 254 VAL VAL A . n 
A 1 141 VAL 141 255 255 VAL VAL A . n 
A 1 142 SER 142 256 256 SER SER A . n 
A 1 143 THR 143 257 257 THR THR A . n 
A 1 144 GLN 144 258 258 GLN GLN A . n 
A 1 145 LEU 145 259 259 LEU LEU A . n 
A 1 146 LEU 146 260 260 LEU LEU A . n 
A 1 147 LEU 147 261 261 LEU LEU A . n 
A 1 148 ASN 148 262 262 ASN ASN A . n 
A 1 149 GLY 149 263 263 GLY GLY A . n 
A 1 150 SER 150 264 264 SER SER A . n 
A 1 151 LEU 151 265 265 LEU LEU A . n 
A 1 152 ALA 152 266 266 ALA ALA A . n 
A 1 153 GLU 153 267 267 GLU GLU A . n 
A 1 154 GLU 154 268 268 GLU GLU A . n 
A 1 155 GLU 155 269 269 GLU GLU A . n 
A 1 156 ILE 156 270 270 ILE ILE A . n 
A 1 157 ILE 157 271 271 ILE ILE A . n 
A 1 158 ILE 158 272 272 ILE ILE A . n 
A 1 159 ARG 159 273 273 ARG ARG A . n 
A 1 160 SER 160 274 274 SER SER A . n 
A 1 161 GLU 161 275 275 GLU GLU A . n 
A 1 162 ASN 162 276 276 ASN ASN A . n 
A 1 163 LEU 163 277 277 LEU LEU A . n 
A 1 164 THR 164 278 278 THR THR A . n 
A 1 165 ASN 165 279 279 ASN ASN A . n 
A 1 166 ASN 166 280 280 ASN ASN A . n 
A 1 167 ALA 167 281 281 ALA ALA A . n 
A 1 168 LYS 168 282 282 LYS LYS A . n 
A 1 169 THR 169 283 283 THR THR A . n 
A 1 170 ILE 170 284 284 ILE ILE A . n 
A 1 171 ILE 171 285 285 ILE ILE A . n 
A 1 172 VAL 172 286 286 VAL VAL A . n 
A 1 173 HIS 173 287 287 HIS HIS A . n 
A 1 174 LEU 174 288 288 LEU LEU A . n 
A 1 175 ASN 175 289 289 ASN ASN A . n 
A 1 176 LYS 176 290 290 LYS LYS A . n 
A 1 177 SER 177 291 291 SER SER A . n 
A 1 178 VAL 178 292 292 VAL VAL A . n 
A 1 179 GLU 179 293 293 GLU GLU A . n 
A 1 180 ILE 180 294 294 ILE ILE A . n 
A 1 181 ASN 181 295 295 ASN ASN A . n 
A 1 182 CYS 182 296 296 CYS CYS A . n 
A 1 183 THR 183 297 297 THR THR A . n 
A 1 184 ARG 184 298 298 ARG ARG A . n 
A 1 185 PRO 185 299 299 PRO PRO A . n 
A 1 186 SER 186 300 300 SER SER A . n 
A 1 187 ASN 187 301 301 ASN ASN A . n 
A 1 188 GLY 188 318 ?   ?   ?   A . n 
A 1 189 GLY 189 319 ?   ?   ?   A . n 
A 1 190 SER 190 320 ?   ?   ?   A . n 
A 1 191 GLY 191 321 ?   ?   ?   A . n 
A 1 192 SER 192 322 ?   ?   ?   A . n 
A 1 193 GLY 193 323 ?   ?   ?   A . n 
A 1 194 GLY 194 324 ?   ?   ?   A . n 
A 1 195 ASP 195 325 325 ASP ASP A . n 
A 1 196 ILE 196 326 326 ILE ILE A . n 
A 1 197 ARG 197 327 327 ARG ARG A . n 
A 1 198 LYS 198 328 328 LYS LYS A . n 
A 1 199 ALA 199 329 329 ALA ALA A . n 
A 1 200 TYR 200 330 330 TYR TYR A . n 
A 1 201 CYS 201 331 331 CYS CYS A . n 
A 1 202 GLU 202 332 332 GLU GLU A . n 
A 1 203 ILE 203 333 333 ILE ILE A . n 
A 1 204 ASN 204 334 334 ASN ASN A . n 
A 1 205 GLY 205 335 335 GLY GLY A . n 
A 1 206 THR 206 336 336 THR THR A . n 
A 1 207 LYS 207 337 337 LYS LYS A . n 
A 1 208 TRP 208 338 338 TRP TRP A . n 
A 1 209 ASN 209 339 339 ASN ASN A . n 
A 1 210 LYS 210 340 340 LYS LYS A . n 
A 1 211 VAL 211 341 341 VAL VAL A . n 
A 1 212 LEU 212 342 342 LEU LEU A . n 
A 1 213 LYS 213 343 343 LYS LYS A . n 
A 1 214 GLN 214 344 344 GLN GLN A . n 
A 1 215 VAL 215 345 345 VAL VAL A . n 
A 1 216 THR 216 346 346 THR THR A . n 
A 1 217 GLU 217 347 347 GLU GLU A . n 
A 1 218 LYS 218 348 348 LYS LYS A . n 
A 1 219 LEU 219 349 349 LEU LEU A . n 
A 1 220 LYS 220 350 350 LYS LYS A . n 
A 1 221 GLU 221 351 351 GLU GLU A . n 
A 1 222 HIS 222 352 352 HIS HIS A . n 
A 1 223 PHE 223 353 353 PHE PHE A . n 
A 1 224 ASN 224 354 354 ASN ASN A . n 
A 1 225 ASN 225 355 355 ASN ASN A . n 
A 1 226 LYS 226 357 357 LYS LYS A . n 
A 1 227 THR 227 358 358 THR THR A . n 
A 1 228 ILE 228 359 359 ILE ILE A . n 
A 1 229 ILE 229 360 360 ILE ILE A . n 
A 1 230 PHE 230 361 361 PHE PHE A . n 
A 1 231 GLN 231 362 362 GLN GLN A . n 
A 1 232 PRO 232 363 363 PRO PRO A . n 
A 1 233 PRO 233 364 364 PRO PRO A . n 
A 1 234 SER 234 365 365 SER SER A . n 
A 1 235 GLY 235 366 366 GLY GLY A . n 
A 1 236 GLY 236 367 367 GLY GLY A . n 
A 1 237 ASP 237 368 368 ASP ASP A . n 
A 1 238 LEU 238 369 369 LEU LEU A . n 
A 1 239 GLU 239 370 370 GLU GLU A . n 
A 1 240 ILE 240 371 371 ILE ILE A . n 
A 1 241 THR 241 372 372 THR THR A . n 
A 1 242 MET 242 373 373 MET MET A . n 
A 1 243 HIS 243 374 374 HIS HIS A . n 
A 1 244 SER 244 375 375 SER SER A . n 
A 1 245 PHE 245 376 376 PHE PHE A . n 
A 1 246 ASN 246 377 377 ASN ASN A . n 
A 1 247 CYS 247 378 378 CYS CYS A . n 
A 1 248 ARG 248 379 379 ARG ARG A . n 
A 1 249 GLY 249 380 380 GLY GLY A . n 
A 1 250 GLU 250 381 381 GLU GLU A . n 
A 1 251 PHE 251 382 382 PHE PHE A . n 
A 1 252 PHE 252 383 383 PHE PHE A . n 
A 1 253 TYR 253 384 384 TYR TYR A . n 
A 1 254 CYS 254 385 385 CYS CYS A . n 
A 1 255 ASN 255 386 386 ASN ASN A . n 
A 1 256 THR 256 387 387 THR THR A . n 
A 1 257 THR 257 388 388 THR THR A . n 
A 1 258 GLN 258 389 389 GLN GLN A . n 
A 1 259 LEU 259 390 390 LEU LEU A . n 
A 1 260 PHE 260 391 391 PHE PHE A . n 
A 1 261 ASN 261 392 392 ASN ASN A . n 
A 1 262 ASN 262 393 393 ASN ASN A . n 
A 1 263 THR 263 394 394 THR THR A . n 
A 1 264 CYS 264 395 395 CYS CYS A . n 
A 1 265 ILE 265 402 ?   ?   ?   A . n 
A 1 266 GLY 266 403 ?   ?   ?   A . n 
A 1 267 ASN 267 404 ?   ?   ?   A . n 
A 1 268 GLU 268 405 ?   ?   ?   A . n 
A 1 269 THR 269 406 ?   ?   ?   A . n 
A 1 270 MET 270 407 ?   ?   ?   A . n 
A 1 271 LYS 271 408 ?   ?   ?   A . n 
A 1 272 GLY 272 409 409 GLY GLY A . n 
A 1 273 CYS 273 410 410 CYS CYS A . n 
A 1 274 ASN 274 411 411 ASN ASN A . n 
A 1 275 GLY 275 412 412 GLY GLY A . n 
A 1 276 THR 276 413 413 THR THR A . n 
A 1 277 ILE 277 414 414 ILE ILE A . n 
A 1 278 THR 278 415 415 THR THR A . n 
A 1 279 LEU 279 416 416 LEU LEU A . n 
A 1 280 PRO 280 417 417 PRO PRO A . n 
A 1 281 CYS 281 418 418 CYS CYS A . n 
A 1 282 LYS 282 419 419 LYS LYS A . n 
A 1 283 ILE 283 420 420 ILE ILE A . n 
A 1 284 LYS 284 421 421 LYS LYS A . n 
A 1 285 GLN 285 422 422 GLN GLN A . n 
A 1 286 ILE 286 423 423 ILE ILE A . n 
A 1 287 ILE 287 424 424 ILE ILE A . n 
A 1 288 ASN 288 425 425 ASN ASN A . n 
A 1 289 MET 289 426 426 MET MET A . n 
A 1 290 TRP 290 427 427 TRP TRP A . n 
A 1 291 GLN 291 428 428 GLN GLN A . n 
A 1 292 GLY 292 429 429 GLY GLY A . n 
A 1 293 THR 293 430 430 THR THR A . n 
A 1 294 GLY 294 431 431 GLY GLY A . n 
A 1 295 GLN 295 432 432 GLN GLN A . n 
A 1 296 ALA 296 433 433 ALA ALA A . n 
A 1 297 MET 297 434 434 MET MET A . n 
A 1 298 TYR 298 435 435 TYR TYR A . n 
A 1 299 ALA 299 436 436 ALA ALA A . n 
A 1 300 PRO 300 437 437 PRO PRO A . n 
A 1 301 PRO 301 438 438 PRO PRO A . n 
A 1 302 ILE 302 439 439 ILE ILE A . n 
A 1 303 ASP 303 440 440 ASP ASP A . n 
A 1 304 GLY 304 441 441 GLY GLY A . n 
A 1 305 LYS 305 442 442 LYS LYS A . n 
A 1 306 ILE 306 443 443 ILE ILE A . n 
A 1 307 ASN 307 444 444 ASN ASN A . n 
A 1 308 CYS 308 445 445 CYS CYS A . n 
A 1 309 VAL 309 446 446 VAL VAL A . n 
A 1 310 SER 310 447 447 SER SER A . n 
A 1 311 ASN 311 448 448 ASN ASN A . n 
A 1 312 ILE 312 449 449 ILE ILE A . n 
A 1 313 THR 313 450 450 THR THR A . n 
A 1 314 GLY 314 451 451 GLY GLY A . n 
A 1 315 ILE 315 452 452 ILE ILE A . n 
A 1 316 LEU 316 453 453 LEU LEU A . n 
A 1 317 LEU 317 454 454 LEU LEU A . n 
A 1 318 THR 318 455 455 THR THR A . n 
A 1 319 ARG 319 456 456 ARG ARG A . n 
A 1 320 ASP 320 457 457 ASP ASP A . n 
A 1 321 GLY 321 458 458 GLY GLY A . n 
A 1 322 GLY 322 459 459 GLY GLY A . n 
A 1 323 ALA 323 460 460 ALA ALA A . n 
A 1 324 ASN 324 461 461 ASN ASN A . n 
A 1 325 ASN 325 462 462 ASN ASN A . n 
A 1 326 THR 326 463 463 THR THR A . n 
A 1 327 SER 327 464 464 SER SER A . n 
A 1 328 ASN 328 465 465 ASN ASN A . n 
A 1 329 GLU 329 466 466 GLU GLU A . n 
A 1 330 THR 330 467 467 THR THR A . n 
A 1 331 PHE 331 468 468 PHE PHE A . n 
A 1 332 ARG 332 469 469 ARG ARG A . n 
A 1 333 PRO 333 470 470 PRO PRO A . n 
A 1 334 GLY 334 471 471 GLY GLY A . n 
A 1 335 GLY 335 472 472 GLY GLY A . n 
A 1 336 GLY 336 473 473 GLY GLY A . n 
A 1 337 ASP 337 474 474 ASP ASP A . n 
A 1 338 MET 338 475 475 MET MET A . n 
A 1 339 ARG 339 476 476 ARG ARG A . n 
A 1 340 ASP 340 477 477 ASP ASP A . n 
A 1 341 ASN 341 478 478 ASN ASN A . n 
A 1 342 TRP 342 479 479 TRP TRP A . n 
A 1 343 ARG 343 480 480 ARG ARG A . n 
A 1 344 SER 344 481 481 SER SER A . n 
A 1 345 GLU 345 482 482 GLU GLU A . n 
A 1 346 LEU 346 483 483 LEU LEU A . n 
A 1 347 TYR 347 484 484 TYR TYR A . n 
A 1 348 LYS 348 485 485 LYS LYS A . n 
A 1 349 TYR 349 486 486 TYR TYR A . n 
A 1 350 LYS 350 487 487 LYS LYS A . n 
A 1 351 VAL 351 488 488 VAL VAL A . n 
A 1 352 VAL 352 489 489 VAL VAL A . n 
A 1 353 GLN 353 490 490 GLN GLN A . n 
A 1 354 ILE 354 491 491 ILE ILE A . n 
A 1 355 GLU 355 492 492 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ATK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATK 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG   1   501 501 NAG   NAG A . 
C 2 NAG   1   502 502 NAG   NAG A . 
D 2 NAG   1   503 503 NAG   NAG A . 
E 2 NAG   1   504 504 NAG   NAG A . 
F 2 NAG   1   505 505 NAG   NAG A . 
G 2 NAG   1   506 506 NAG   NAG A . 
H 2 NAG   1   507 507 NAG   NAG A . 
I 2 NAG   1   508 508 NAG   NAG A . 
J 2 NAG   1   509 510 NAG   NAG A . 
K 3 EPE   1   510 512 EPE   EPE A . 
L 4 A1ATK 1   511 1   A1ATK MW5 A . 
M 5 MPD   1   512 1   MPD   MPD A . 
N 6 HOH   1   601 34  HOH   HOH A . 
N 6 HOH   2   602 85  HOH   HOH A . 
N 6 HOH   3   603 129 HOH   HOH A . 
N 6 HOH   4   604 125 HOH   HOH A . 
N 6 HOH   5   605 155 HOH   HOH A . 
N 6 HOH   6   606 173 HOH   HOH A . 
N 6 HOH   7   607 53  HOH   HOH A . 
N 6 HOH   8   608 110 HOH   HOH A . 
N 6 HOH   9   609 131 HOH   HOH A . 
N 6 HOH   10  610 35  HOH   HOH A . 
N 6 HOH   11  611 16  HOH   HOH A . 
N 6 HOH   12  612 89  HOH   HOH A . 
N 6 HOH   13  613 67  HOH   HOH A . 
N 6 HOH   14  614 170 HOH   HOH A . 
N 6 HOH   15  615 156 HOH   HOH A . 
N 6 HOH   16  616 106 HOH   HOH A . 
N 6 HOH   17  617 10  HOH   HOH A . 
N 6 HOH   18  618 75  HOH   HOH A . 
N 6 HOH   19  619 120 HOH   HOH A . 
N 6 HOH   20  620 138 HOH   HOH A . 
N 6 HOH   21  621 149 HOH   HOH A . 
N 6 HOH   22  622 66  HOH   HOH A . 
N 6 HOH   23  623 8   HOH   HOH A . 
N 6 HOH   24  624 36  HOH   HOH A . 
N 6 HOH   25  625 40  HOH   HOH A . 
N 6 HOH   26  626 88  HOH   HOH A . 
N 6 HOH   27  627 28  HOH   HOH A . 
N 6 HOH   28  628 42  HOH   HOH A . 
N 6 HOH   29  629 103 HOH   HOH A . 
N 6 HOH   30  630 160 HOH   HOH A . 
N 6 HOH   31  631 79  HOH   HOH A . 
N 6 HOH   32  632 24  HOH   HOH A . 
N 6 HOH   33  633 78  HOH   HOH A . 
N 6 HOH   34  634 114 HOH   HOH A . 
N 6 HOH   35  635 9   HOH   HOH A . 
N 6 HOH   36  636 100 HOH   HOH A . 
N 6 HOH   37  637 23  HOH   HOH A . 
N 6 HOH   38  638 73  HOH   HOH A . 
N 6 HOH   39  639 121 HOH   HOH A . 
N 6 HOH   40  640 41  HOH   HOH A . 
N 6 HOH   41  641 72  HOH   HOH A . 
N 6 HOH   42  642 84  HOH   HOH A . 
N 6 HOH   43  643 1   HOH   HOH A . 
N 6 HOH   44  644 31  HOH   HOH A . 
N 6 HOH   45  645 6   HOH   HOH A . 
N 6 HOH   46  646 117 HOH   HOH A . 
N 6 HOH   47  647 27  HOH   HOH A . 
N 6 HOH   48  648 56  HOH   HOH A . 
N 6 HOH   49  649 183 HOH   HOH A . 
N 6 HOH   50  650 96  HOH   HOH A . 
N 6 HOH   51  651 81  HOH   HOH A . 
N 6 HOH   52  652 43  HOH   HOH A . 
N 6 HOH   53  653 22  HOH   HOH A . 
N 6 HOH   54  654 49  HOH   HOH A . 
N 6 HOH   55  655 172 HOH   HOH A . 
N 6 HOH   56  656 152 HOH   HOH A . 
N 6 HOH   57  657 59  HOH   HOH A . 
N 6 HOH   58  658 45  HOH   HOH A . 
N 6 HOH   59  659 157 HOH   HOH A . 
N 6 HOH   60  660 47  HOH   HOH A . 
N 6 HOH   61  661 19  HOH   HOH A . 
N 6 HOH   62  662 102 HOH   HOH A . 
N 6 HOH   63  663 167 HOH   HOH A . 
N 6 HOH   64  664 20  HOH   HOH A . 
N 6 HOH   65  665 97  HOH   HOH A . 
N 6 HOH   66  666 118 HOH   HOH A . 
N 6 HOH   67  667 12  HOH   HOH A . 
N 6 HOH   68  668 33  HOH   HOH A . 
N 6 HOH   69  669 139 HOH   HOH A . 
N 6 HOH   70  670 77  HOH   HOH A . 
N 6 HOH   71  671 168 HOH   HOH A . 
N 6 HOH   72  672 169 HOH   HOH A . 
N 6 HOH   73  673 105 HOH   HOH A . 
N 6 HOH   74  674 113 HOH   HOH A . 
N 6 HOH   75  675 52  HOH   HOH A . 
N 6 HOH   76  676 50  HOH   HOH A . 
N 6 HOH   77  677 26  HOH   HOH A . 
N 6 HOH   78  678 107 HOH   HOH A . 
N 6 HOH   79  679 3   HOH   HOH A . 
N 6 HOH   80  680 37  HOH   HOH A . 
N 6 HOH   81  681 92  HOH   HOH A . 
N 6 HOH   82  682 7   HOH   HOH A . 
N 6 HOH   83  683 14  HOH   HOH A . 
N 6 HOH   84  684 17  HOH   HOH A . 
N 6 HOH   85  685 5   HOH   HOH A . 
N 6 HOH   86  686 44  HOH   HOH A . 
N 6 HOH   87  687 15  HOH   HOH A . 
N 6 HOH   88  688 69  HOH   HOH A . 
N 6 HOH   89  689 32  HOH   HOH A . 
N 6 HOH   90  690 39  HOH   HOH A . 
N 6 HOH   91  691 58  HOH   HOH A . 
N 6 HOH   92  692 38  HOH   HOH A . 
N 6 HOH   93  693 101 HOH   HOH A . 
N 6 HOH   94  694 93  HOH   HOH A . 
N 6 HOH   95  695 186 HOH   HOH A . 
N 6 HOH   96  696 11  HOH   HOH A . 
N 6 HOH   97  697 65  HOH   HOH A . 
N 6 HOH   98  698 80  HOH   HOH A . 
N 6 HOH   99  699 61  HOH   HOH A . 
N 6 HOH   100 700 133 HOH   HOH A . 
N 6 HOH   101 701 4   HOH   HOH A . 
N 6 HOH   102 702 60  HOH   HOH A . 
N 6 HOH   103 703 13  HOH   HOH A . 
N 6 HOH   104 704 48  HOH   HOH A . 
N 6 HOH   105 705 142 HOH   HOH A . 
N 6 HOH   106 706 51  HOH   HOH A . 
N 6 HOH   107 707 64  HOH   HOH A . 
N 6 HOH   108 708 159 HOH   HOH A . 
N 6 HOH   109 709 135 HOH   HOH A . 
N 6 HOH   110 710 119 HOH   HOH A . 
N 6 HOH   111 711 2   HOH   HOH A . 
N 6 HOH   112 712 46  HOH   HOH A . 
N 6 HOH   113 713 18  HOH   HOH A . 
N 6 HOH   114 714 76  HOH   HOH A . 
N 6 HOH   115 715 62  HOH   HOH A . 
N 6 HOH   116 716 146 HOH   HOH A . 
N 6 HOH   117 717 151 HOH   HOH A . 
N 6 HOH   118 718 143 HOH   HOH A . 
N 6 HOH   119 719 30  HOH   HOH A . 
N 6 HOH   120 720 82  HOH   HOH A . 
N 6 HOH   121 721 136 HOH   HOH A . 
N 6 HOH   122 722 122 HOH   HOH A . 
N 6 HOH   123 723 57  HOH   HOH A . 
N 6 HOH   124 724 29  HOH   HOH A . 
N 6 HOH   125 725 127 HOH   HOH A . 
N 6 HOH   126 726 141 HOH   HOH A . 
N 6 HOH   127 727 132 HOH   HOH A . 
N 6 HOH   128 728 134 HOH   HOH A . 
N 6 HOH   129 729 70  HOH   HOH A . 
N 6 HOH   130 730 185 HOH   HOH A . 
N 6 HOH   131 731 21  HOH   HOH A . 
N 6 HOH   132 732 128 HOH   HOH A . 
N 6 HOH   133 733 124 HOH   HOH A . 
N 6 HOH   134 734 55  HOH   HOH A . 
N 6 HOH   135 735 63  HOH   HOH A . 
N 6 HOH   136 736 184 HOH   HOH A . 
N 6 HOH   137 737 162 HOH   HOH A . 
N 6 HOH   138 738 180 HOH   HOH A . 
N 6 HOH   139 739 99  HOH   HOH A . 
N 6 HOH   140 740 164 HOH   HOH A . 
N 6 HOH   141 741 115 HOH   HOH A . 
N 6 HOH   142 742 25  HOH   HOH A . 
N 6 HOH   143 743 68  HOH   HOH A . 
N 6 HOH   144 744 90  HOH   HOH A . 
N 6 HOH   145 745 54  HOH   HOH A . 
N 6 HOH   146 746 161 HOH   HOH A . 
N 6 HOH   147 747 166 HOH   HOH A . 
N 6 HOH   148 748 179 HOH   HOH A . 
N 6 HOH   149 749 104 HOH   HOH A . 
N 6 HOH   150 750 74  HOH   HOH A . 
N 6 HOH   151 751 177 HOH   HOH A . 
N 6 HOH   152 752 95  HOH   HOH A . 
N 6 HOH   153 753 165 HOH   HOH A . 
N 6 HOH   154 754 175 HOH   HOH A . 
N 6 HOH   155 755 147 HOH   HOH A . 
N 6 HOH   156 756 181 HOH   HOH A . 
N 6 HOH   157 757 176 HOH   HOH A . 
N 6 HOH   158 758 91  HOH   HOH A . 
N 6 HOH   159 759 153 HOH   HOH A . 
N 6 HOH   160 760 145 HOH   HOH A . 
N 6 HOH   161 761 109 HOH   HOH A . 
N 6 HOH   162 762 116 HOH   HOH A . 
N 6 HOH   163 763 86  HOH   HOH A . 
N 6 HOH   164 764 163 HOH   HOH A . 
N 6 HOH   165 765 111 HOH   HOH A . 
N 6 HOH   166 766 137 HOH   HOH A . 
N 6 HOH   167 767 174 HOH   HOH A . 
N 6 HOH   168 768 150 HOH   HOH A . 
N 6 HOH   169 769 123 HOH   HOH A . 
N 6 HOH   170 770 130 HOH   HOH A . 
N 6 HOH   171 771 83  HOH   HOH A . 
N 6 HOH   172 772 98  HOH   HOH A . 
N 6 HOH   173 773 148 HOH   HOH A . 
N 6 HOH   174 774 94  HOH   HOH A . 
N 6 HOH   175 775 71  HOH   HOH A . 
N 6 HOH   176 776 158 HOH   HOH A . 
N 6 HOH   177 777 140 HOH   HOH A . 
N 6 HOH   178 778 154 HOH   HOH A . 
N 6 HOH   179 779 144 HOH   HOH A . 
N 6 HOH   180 780 178 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BXD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.013 
_cell.length_a_esd                 ? 
_cell.length_b                     65.837 
_cell.length_b_esd                 ? 
_cell.length_c                     90.518 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BXD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BXD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10% PEG 3350
5% PEG 400
0.1 M HEPES pH 7.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'SI(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95369 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95369 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BXD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     29237 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           92.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.043 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.065 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.88 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1143 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               1.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.526 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.5 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          74.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.636 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BXD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             27.43 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     29202 
_refine.ls_number_reflns_R_free                  1457 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.34 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2311 
_refine.ls_R_factor_R_free                       0.2591 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2297 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.65 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2659 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         185 
_refine_hist.number_atoms_solvent             180 
_refine_hist.number_atoms_total               3024 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        27.43 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 2901 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.997  ? 3939 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.326 ? 433  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 462  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 493  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.85 1.92  . . 120 2270 77.00 . . . . 0.3552 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 1.92 2.00  . . 132 2512 85.00 . . . . 0.3173 . . . . . . . . . . . 0.3532 
'X-RAY DIFFRACTION' 2.00 2.09  . . 125 2554 86.00 . . . . 0.2987 . . . . . . . . . . . 0.3585 
'X-RAY DIFFRACTION' 2.09 2.20  . . 142 2899 97.00 . . . . 0.2852 . . . . . . . . . . . 0.3087 
'X-RAY DIFFRACTION' 2.20 2.33  . . 172 2919 99.00 . . . . 0.2783 . . . . . . . . . . . 0.2950 
'X-RAY DIFFRACTION' 2.34 2.52  . . 181 2923 99.00 . . . . 0.2674 . . . . . . . . . . . 0.2730 
'X-RAY DIFFRACTION' 2.52 2.77  . . 142 2943 98.00 . . . . 0.2559 . . . . . . . . . . . 0.3116 
'X-RAY DIFFRACTION' 2.77 3.17  . . 124 2890 95.00 . . . . 0.2393 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 3.17 3.99  . . 167 2937 97.00 . . . . 0.2085 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 3.99 27.43 . . 152 2898 91.00 . . . . 0.1897 . . . . . . . . . . . 0.2171 
# 
_struct.entry_id                     9BXD 
_struct.title                        'CRYSTAL STRUCTURE OF HIV-1 LM/HS CLADE A/E CRF01 GP120 CORE IN COMPLEX WITH HZ-IV-188' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BXD 
_struct_keywords.text            'HIV-1 GP120, CLADE A/E CF01, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0M3KKW9_9HIV1 
_struct_ref.pdbx_db_accession          A0A0M3KKW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT
GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN
LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM
HHFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG
ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BXD 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 355 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0M3KKW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  353 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       44 
_struct_ref_seq.pdbx_auth_seq_align_end       492 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BXD VAL A 1   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      42  1 
1 9BXD PRO A 2   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      43  2 
1 9BXD TYR A 20  ? UNP A0A0M3KKW9 HIS 18  'engineered mutation' 61  3 
1 9BXD HIS A 64  ? UNP A0A0M3KKW9 GLN 62  'engineered mutation' 105 4 
1 9BXD ILE A 67  ? UNP A0A0M3KKW9 VAL 65  'engineered mutation' 108 5 
1 9BXD SER A 244 ? UNP A0A0M3KKW9 HIS 242 'engineered mutation' 375 6 
1 9BXD ASP A 337 ? UNP A0A0M3KKW9 ASN 335 'engineered mutation' 474 7 
1 9BXD MET A 338 ? UNP A0A0M3KKW9 ILE 336 'engineered mutation' 475 8 
1 9BXD ARG A 339 ? UNP A0A0M3KKW9 LYS 337 'engineered mutation' 476 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 23  ? CYS A 33  ? GLU A 64  CYS A 74  1 ? 11 
HELX_P HELX_P2 AA2 ASN A 57  ? LEU A 75  ? ASN A 98  LEU A 116 1 ? 19 
HELX_P HELX_P3 AA3 THR A 82  ? SER A 85  ? THR A 123 SER A 199 5 ? 4  
HELX_P HELX_P4 AA4 GLY A 205 ? PHE A 223 ? GLY A 335 PHE A 353 1 ? 19 
HELX_P HELX_P5 AA5 ASP A 237 ? MET A 242 ? ASP A 368 MET A 373 1 ? 6  
HELX_P HELX_P6 AA6 MET A 338 ? TYR A 347 ? MET A 475 TYR A 484 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 13  SG  ? ? ? 1_555 A CYS 33  SG ? ? A CYS 54  A CYS 74  1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf2 disulf ?   ? A CYS 78  SG  ? ? ? 1_555 A CYS 91  SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.019 ? ?               
disulf3 disulf ?   ? A CYS 104 SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf4 disulf ?   ? A CYS 114 SG  ? ? ? 1_555 A CYS 125 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf5 disulf ?   ? A CYS 182 SG  ? ? ? 1_555 A CYS 201 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf6 disulf ?   ? A CYS 247 SG  ? ? ? 1_555 A CYS 308 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.026 ? ?               
disulf7 disulf ?   ? A CYS 254 SG  ? ? ? 1_555 A CYS 281 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf8 disulf ?   ? A CYS 264 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 2.020 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 234 A NAG 501 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale2 covale one ? A ASN 127 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 241 A NAG 502 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale3 covale one ? A ASN 148 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 262 A NAG 503 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
covale4 covale one ? A ASN 162 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 276 A NAG 504 1_555 ? ? ? ? ? ? ? 1.428 ? N-Glycosylation 
covale5 covale one ? A ASN 175 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 289 A NAG 505 1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale6 covale one ? A ASN 181 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 506 1_555 ? ? ? ? ? ? ? 1.429 ? N-Glycosylation 
covale7 covale one ? A ASN 204 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 334 A NAG 507 1_555 ? ? ? ? ? ? ? 1.426 ? N-Glycosylation 
covale8 covale one ? A ASN 255 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 386 A NAG 508 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale9 covale one ? A ASN 311 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 448 A NAG 509 1_555 ? ? ? ? ? ? ? 1.426 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG B .   ? ASN A 120 ? NAG A 501 ? 1_555 ASN A 234 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 127 ? NAG A 502 ? 1_555 ASN A 241 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 148 ? NAG A 503 ? 1_555 ASN A 262 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 162 ? NAG A 504 ? 1_555 ASN A 276 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 175 ? NAG A 505 ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 181 ? NAG A 506 ? 1_555 ASN A 295 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 204 ? NAG A 507 ? 1_555 ASN A 334 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I .   ? ASN A 255 ? NAG A 508 ? 1_555 ASN A 386 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG J .   ? ASN A 311 ? NAG A 509 ? 1_555 ASN A 448 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 CYS A 13  ? CYS A 33  ? CYS A 54  ? 1_555 CYS A 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 78  ? CYS A 91  ? CYS A 119 ? 1_555 CYS A 205 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 104 ? CYS A 133 ? CYS A 218 ? 1_555 CYS A 247 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 114 ? CYS A 125 ? CYS A 228 ? 1_555 CYS A 239 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 182 ? CYS A 201 ? CYS A 296 ? 1_555 CYS A 331 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 247 ? CYS A 308 ? CYS A 378 ? 1_555 CYS A 445 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 254 ? CYS A 281 ? CYS A 385 ? 1_555 CYS A 418 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 264 ? CYS A 273 ? CYS A 395 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 4   ? ASP A 6   ? TRP A 45  ASP A 47  
AA1 2 TYR A 349 ? ILE A 354 ? TYR A 486 ILE A 491 
AA1 3 TYR A 109 ? CYS A 114 ? TYR A 223 CYS A 228 
AA1 4 VAL A 128 ? VAL A 131 ? VAL A 242 VAL A 245 
AA1 5 ILE A 43  ? HIS A 44  ? ILE A 84  HIS A 85  
AA2 1 VAL A 34  ? PRO A 35  ? VAL A 75  PRO A 76  
AA2 2 PHE A 12  ? SER A 15  ? PHE A 53  SER A 56  
AA2 3 HIS A 102 ? CYS A 104 ? HIS A 216 CYS A 218 
AA3 1 GLU A 50  ? ASN A 53  ? GLU A 91  ASN A 94  
AA3 2 THR A 122 ? CYS A 125 ? THR A 236 CYS A 239 
AA4 1 ILE A 87  ? LYS A 88  ? ILE A 201 LYS A 202 
AA4 2 VAL A 79  ? LYS A 80  ? VAL A 120 LYS A 121 
AA4 3 GLN A 295 ? MET A 297 ? GLN A 432 MET A 434 
AA4 4 ILE A 286 ? ASN A 288 ? ILE A 423 ASN A 425 
AA5 1 LEU A 145 ? LEU A 147 ? LEU A 259 LEU A 261 
AA5 2 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA5 3 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA5 4 ASN A 328 ? PRO A 333 ? ASN A 465 PRO A 470 
AA5 5 THR A 227 ? PHE A 230 ? THR A 358 PHE A 361 
AA6 1 ILE A 157 ? ARG A 159 ? ILE A 271 ARG A 273 
AA6 2 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA6 3 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA6 4 LYS A 198 ? ASN A 204 ? LYS A 328 ASN A 334 
AA6 5 THR A 276 ? LYS A 284 ? THR A 413 LYS A 421 
AA6 6 GLU A 250 ? CYS A 254 ? GLU A 381 CYS A 385 
AA6 7 HIS A 243 ? CYS A 247 ? HIS A 374 CYS A 378 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 5   ? N LYS A 46  O GLN A 353 ? O GLN A 490 
AA1 2 3 O LYS A 350 ? O LYS A 487 N LEU A 112 ? N LEU A 226 
AA1 3 4 N LYS A 113 ? N LYS A 227 O SER A 129 ? O SER A 243 
AA1 4 5 O SER A 130 ? O SER A 244 N ILE A 43  ? N ILE A 84  
AA2 1 2 O VAL A 34  ? O VAL A 75  N CYS A 13  ? N CYS A 54  
AA2 2 3 N PHE A 12  ? N PHE A 53  O CYS A 104 ? O CYS A 218 
AA3 1 2 N PHE A 52  ? N PHE A 93  O GLY A 123 ? O GLY A 237 
AA4 1 2 O ILE A 87  ? O ILE A 201 N LYS A 80  ? N LYS A 121 
AA4 2 3 N VAL A 79  ? N VAL A 120 O MET A 297 ? O MET A 434 
AA4 3 4 O ALA A 296 ? O ALA A 433 N ILE A 287 ? N ILE A 424 
AA5 1 2 N LEU A 146 ? N LEU A 260 O THR A 313 ? O THR A 450 
AA5 2 3 O LEU A 317 ? O LEU A 454 N ILE A 170 ? N ILE A 284 
AA5 4 5 O PHE A 331 ? O PHE A 468 N ILE A 229 ? N ILE A 360 
AA6 1 2 N ARG A 159 ? N ARG A 273 O ILE A 171 ? O ILE A 285 
AA6 2 3 N ILE A 170 ? N ILE A 284 O LEU A 317 ? O LEU A 454 
AA6 4 5 N ILE A 203 ? N ILE A 333 O ILE A 277 ? O ILE A 414 
AA6 5 6 O LYS A 284 ? O LYS A 421 N PHE A 251 ? N PHE A 382 
AA6 6 7 O CYS A 254 ? O CYS A 385 N HIS A 243 ? N HIS A 374 
# 
_pdbx_entry_details.entry_id                   9BXD 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 57  ? ? -95.16  33.57  
2  1 TYR A 61  ? ? -164.25 -29.85 
3  1 SER A 115 ? ? -120.65 -51.91 
4  1 THR A 123 ? ? -44.78  109.23 
5  1 ASP A 211 ? ? -162.41 100.67 
6  1 GLN A 258 ? ? 63.65   -56.82 
7  1 GLU A 268 ? ? -112.38 -96.48 
8  1 ASN A 276 ? ? -172.67 95.21  
9  1 PHE A 391 ? ? -99.01  36.80  
10 1 ASN A 411 ? ? -169.23 7.19   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A VAL 42  ? A VAL 1   
2  1 Y 1 A PRO 43  ? A PRO 2   
3  1 Y 1 A GLY 318 ? A GLY 188 
4  1 Y 1 A GLY 319 ? A GLY 189 
5  1 Y 1 A SER 320 ? A SER 190 
6  1 Y 1 A GLY 321 ? A GLY 191 
7  1 Y 1 A SER 322 ? A SER 192 
8  1 Y 1 A GLY 323 ? A GLY 193 
9  1 Y 1 A GLY 324 ? A GLY 194 
10 1 Y 1 A ILE 402 ? A ILE 265 
11 1 Y 1 A GLY 403 ? A GLY 266 
12 1 Y 1 A ASN 404 ? A ASN 267 
13 1 Y 1 A GLU 405 ? A GLU 268 
14 1 Y 1 A THR 406 ? A THR 269 
15 1 Y 1 A MET 407 ? A MET 270 
16 1 Y 1 A LYS 408 ? A LYS 271 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ATK O    O  N N 1   
A1ATK C10  C  N N 2   
A1ATK N    N  N N 3   
A1ATK CA   C  N S 4   
A1ATK CB   C  N N 5   
A1ATK CG   C  N N 6   
A1ATK CD   C  N N 7   
A1ATK NE   N  N N 8   
A1ATK CZ   C  N N 9   
A1ATK NH1  N  N N 10  
A1ATK NH2  N  N N 11  
A1ATK C01  C  N N 12  
A1ATK C03  C  N N 13  
A1ATK C04  C  N N 14  
A1ATK C06  C  N N 15  
A1ATK C08  C  N N 16  
A1ATK C09  C  N S 17  
A1ATK C13  C  Y N 18  
A1ATK C14  C  Y N 19  
A1ATK C15  C  Y N 20  
A1ATK C17  C  Y N 21  
A1ATK C19  C  Y N 22  
A1ATK C20  C  Y N 23  
A1ATK C21  C  N N 24  
A1ATK C22  C  N N 25  
A1ATK C23  C  N N 26  
A1ATK C25  C  N N 27  
A1ATK C26  C  N N 28  
A1ATK F16  F  N N 29  
A1ATK N02  N  N N 30  
A1ATK N05  N  N N 31  
A1ATK N07  N  N N 32  
A1ATK N12  N  N N 33  
A1ATK O11  O  N N 34  
A1ATK O24  O  N N 35  
A1ATK CL1  CL N N 36  
A1ATK H1   H  N N 37  
A1ATK H2   H  N N 38  
A1ATK H4   H  N N 39  
A1ATK H5   H  N N 40  
A1ATK H6   H  N N 41  
A1ATK H7   H  N N 42  
A1ATK H8   H  N N 43  
A1ATK H9   H  N N 44  
A1ATK H10  H  N N 45  
A1ATK H11  H  N N 46  
A1ATK H12  H  N N 47  
A1ATK H13  H  N N 48  
A1ATK H14  H  N N 49  
A1ATK H15  H  N N 50  
A1ATK H16  H  N N 51  
A1ATK H17  H  N N 52  
A1ATK H18  H  N N 53  
A1ATK H19  H  N N 54  
A1ATK H20  H  N N 55  
A1ATK H21  H  N N 56  
A1ATK H22  H  N N 57  
A1ATK H23  H  N N 58  
A1ATK H24  H  N N 59  
A1ATK H25  H  N N 60  
A1ATK H26  H  N N 61  
A1ATK H27  H  N N 62  
A1ATK H28  H  N N 63  
A1ATK H29  H  N N 64  
A1ATK H30  H  N N 65  
A1ATK H31  H  N N 66  
A1ATK H32  H  N N 67  
A1ATK H33  H  N N 68  
A1ATK H34  H  N N 69  
A1ATK H35  H  N N 70  
ALA   N    N  N N 71  
ALA   CA   C  N S 72  
ALA   C    C  N N 73  
ALA   O    O  N N 74  
ALA   CB   C  N N 75  
ALA   OXT  O  N N 76  
ALA   H    H  N N 77  
ALA   H2   H  N N 78  
ALA   HA   H  N N 79  
ALA   HB1  H  N N 80  
ALA   HB2  H  N N 81  
ALA   HB3  H  N N 82  
ALA   HXT  H  N N 83  
ARG   N    N  N N 84  
ARG   CA   C  N S 85  
ARG   C    C  N N 86  
ARG   O    O  N N 87  
ARG   CB   C  N N 88  
ARG   CG   C  N N 89  
ARG   CD   C  N N 90  
ARG   NE   N  N N 91  
ARG   CZ   C  N N 92  
ARG   NH1  N  N N 93  
ARG   NH2  N  N N 94  
ARG   OXT  O  N N 95  
ARG   H    H  N N 96  
ARG   H2   H  N N 97  
ARG   HA   H  N N 98  
ARG   HB2  H  N N 99  
ARG   HB3  H  N N 100 
ARG   HG2  H  N N 101 
ARG   HG3  H  N N 102 
ARG   HD2  H  N N 103 
ARG   HD3  H  N N 104 
ARG   HE   H  N N 105 
ARG   HH11 H  N N 106 
ARG   HH12 H  N N 107 
ARG   HH21 H  N N 108 
ARG   HH22 H  N N 109 
ARG   HXT  H  N N 110 
ASN   N    N  N N 111 
ASN   CA   C  N S 112 
ASN   C    C  N N 113 
ASN   O    O  N N 114 
ASN   CB   C  N N 115 
ASN   CG   C  N N 116 
ASN   OD1  O  N N 117 
ASN   ND2  N  N N 118 
ASN   OXT  O  N N 119 
ASN   H    H  N N 120 
ASN   H2   H  N N 121 
ASN   HA   H  N N 122 
ASN   HB2  H  N N 123 
ASN   HB3  H  N N 124 
ASN   HD21 H  N N 125 
ASN   HD22 H  N N 126 
ASN   HXT  H  N N 127 
ASP   N    N  N N 128 
ASP   CA   C  N S 129 
ASP   C    C  N N 130 
ASP   O    O  N N 131 
ASP   CB   C  N N 132 
ASP   CG   C  N N 133 
ASP   OD1  O  N N 134 
ASP   OD2  O  N N 135 
ASP   OXT  O  N N 136 
ASP   H    H  N N 137 
ASP   H2   H  N N 138 
ASP   HA   H  N N 139 
ASP   HB2  H  N N 140 
ASP   HB3  H  N N 141 
ASP   HD2  H  N N 142 
ASP   HXT  H  N N 143 
CYS   N    N  N N 144 
CYS   CA   C  N R 145 
CYS   C    C  N N 146 
CYS   O    O  N N 147 
CYS   CB   C  N N 148 
CYS   SG   S  N N 149 
CYS   OXT  O  N N 150 
CYS   H    H  N N 151 
CYS   H2   H  N N 152 
CYS   HA   H  N N 153 
CYS   HB2  H  N N 154 
CYS   HB3  H  N N 155 
CYS   HG   H  N N 156 
CYS   HXT  H  N N 157 
EPE   N1   N  N N 158 
EPE   C2   C  N N 159 
EPE   C3   C  N N 160 
EPE   N4   N  N N 161 
EPE   C5   C  N N 162 
EPE   C6   C  N N 163 
EPE   C7   C  N N 164 
EPE   C8   C  N N 165 
EPE   O8   O  N N 166 
EPE   C9   C  N N 167 
EPE   C10  C  N N 168 
EPE   S    S  N N 169 
EPE   O1S  O  N N 170 
EPE   O2S  O  N N 171 
EPE   O3S  O  N N 172 
EPE   H21  H  N N 173 
EPE   H22  H  N N 174 
EPE   H31  H  N N 175 
EPE   H32  H  N N 176 
EPE   H51  H  N N 177 
EPE   H52  H  N N 178 
EPE   H61  H  N N 179 
EPE   H62  H  N N 180 
EPE   H71  H  N N 181 
EPE   H72  H  N N 182 
EPE   H81  H  N N 183 
EPE   H82  H  N N 184 
EPE   HO8  H  N N 185 
EPE   H91  H  N N 186 
EPE   H92  H  N N 187 
EPE   H101 H  N N 188 
EPE   H102 H  N N 189 
EPE   HOS3 H  N N 190 
GLN   N    N  N N 191 
GLN   CA   C  N S 192 
GLN   C    C  N N 193 
GLN   O    O  N N 194 
GLN   CB   C  N N 195 
GLN   CG   C  N N 196 
GLN   CD   C  N N 197 
GLN   OE1  O  N N 198 
GLN   NE2  N  N N 199 
GLN   OXT  O  N N 200 
GLN   H    H  N N 201 
GLN   H2   H  N N 202 
GLN   HA   H  N N 203 
GLN   HB2  H  N N 204 
GLN   HB3  H  N N 205 
GLN   HG2  H  N N 206 
GLN   HG3  H  N N 207 
GLN   HE21 H  N N 208 
GLN   HE22 H  N N 209 
GLN   HXT  H  N N 210 
GLU   N    N  N N 211 
GLU   CA   C  N S 212 
GLU   C    C  N N 213 
GLU   O    O  N N 214 
GLU   CB   C  N N 215 
GLU   CG   C  N N 216 
GLU   CD   C  N N 217 
GLU   OE1  O  N N 218 
GLU   OE2  O  N N 219 
GLU   OXT  O  N N 220 
GLU   H    H  N N 221 
GLU   H2   H  N N 222 
GLU   HA   H  N N 223 
GLU   HB2  H  N N 224 
GLU   HB3  H  N N 225 
GLU   HG2  H  N N 226 
GLU   HG3  H  N N 227 
GLU   HE2  H  N N 228 
GLU   HXT  H  N N 229 
GLY   N    N  N N 230 
GLY   CA   C  N N 231 
GLY   C    C  N N 232 
GLY   O    O  N N 233 
GLY   OXT  O  N N 234 
GLY   H    H  N N 235 
GLY   H2   H  N N 236 
GLY   HA2  H  N N 237 
GLY   HA3  H  N N 238 
GLY   HXT  H  N N 239 
HIS   N    N  N N 240 
HIS   CA   C  N S 241 
HIS   C    C  N N 242 
HIS   O    O  N N 243 
HIS   CB   C  N N 244 
HIS   CG   C  Y N 245 
HIS   ND1  N  Y N 246 
HIS   CD2  C  Y N 247 
HIS   CE1  C  Y N 248 
HIS   NE2  N  Y N 249 
HIS   OXT  O  N N 250 
HIS   H    H  N N 251 
HIS   H2   H  N N 252 
HIS   HA   H  N N 253 
HIS   HB2  H  N N 254 
HIS   HB3  H  N N 255 
HIS   HD1  H  N N 256 
HIS   HD2  H  N N 257 
HIS   HE1  H  N N 258 
HIS   HE2  H  N N 259 
HIS   HXT  H  N N 260 
HOH   O    O  N N 261 
HOH   H1   H  N N 262 
HOH   H2   H  N N 263 
ILE   N    N  N N 264 
ILE   CA   C  N S 265 
ILE   C    C  N N 266 
ILE   O    O  N N 267 
ILE   CB   C  N S 268 
ILE   CG1  C  N N 269 
ILE   CG2  C  N N 270 
ILE   CD1  C  N N 271 
ILE   OXT  O  N N 272 
ILE   H    H  N N 273 
ILE   H2   H  N N 274 
ILE   HA   H  N N 275 
ILE   HB   H  N N 276 
ILE   HG12 H  N N 277 
ILE   HG13 H  N N 278 
ILE   HG21 H  N N 279 
ILE   HG22 H  N N 280 
ILE   HG23 H  N N 281 
ILE   HD11 H  N N 282 
ILE   HD12 H  N N 283 
ILE   HD13 H  N N 284 
ILE   HXT  H  N N 285 
LEU   N    N  N N 286 
LEU   CA   C  N S 287 
LEU   C    C  N N 288 
LEU   O    O  N N 289 
LEU   CB   C  N N 290 
LEU   CG   C  N N 291 
LEU   CD1  C  N N 292 
LEU   CD2  C  N N 293 
LEU   OXT  O  N N 294 
LEU   H    H  N N 295 
LEU   H2   H  N N 296 
LEU   HA   H  N N 297 
LEU   HB2  H  N N 298 
LEU   HB3  H  N N 299 
LEU   HG   H  N N 300 
LEU   HD11 H  N N 301 
LEU   HD12 H  N N 302 
LEU   HD13 H  N N 303 
LEU   HD21 H  N N 304 
LEU   HD22 H  N N 305 
LEU   HD23 H  N N 306 
LEU   HXT  H  N N 307 
LYS   N    N  N N 308 
LYS   CA   C  N S 309 
LYS   C    C  N N 310 
LYS   O    O  N N 311 
LYS   CB   C  N N 312 
LYS   CG   C  N N 313 
LYS   CD   C  N N 314 
LYS   CE   C  N N 315 
LYS   NZ   N  N N 316 
LYS   OXT  O  N N 317 
LYS   H    H  N N 318 
LYS   H2   H  N N 319 
LYS   HA   H  N N 320 
LYS   HB2  H  N N 321 
LYS   HB3  H  N N 322 
LYS   HG2  H  N N 323 
LYS   HG3  H  N N 324 
LYS   HD2  H  N N 325 
LYS   HD3  H  N N 326 
LYS   HE2  H  N N 327 
LYS   HE3  H  N N 328 
LYS   HZ1  H  N N 329 
LYS   HZ2  H  N N 330 
LYS   HZ3  H  N N 331 
LYS   HXT  H  N N 332 
MET   N    N  N N 333 
MET   CA   C  N S 334 
MET   C    C  N N 335 
MET   O    O  N N 336 
MET   CB   C  N N 337 
MET   CG   C  N N 338 
MET   SD   S  N N 339 
MET   CE   C  N N 340 
MET   OXT  O  N N 341 
MET   H    H  N N 342 
MET   H2   H  N N 343 
MET   HA   H  N N 344 
MET   HB2  H  N N 345 
MET   HB3  H  N N 346 
MET   HG2  H  N N 347 
MET   HG3  H  N N 348 
MET   HE1  H  N N 349 
MET   HE2  H  N N 350 
MET   HE3  H  N N 351 
MET   HXT  H  N N 352 
MPD   C1   C  N N 353 
MPD   C2   C  N N 354 
MPD   O2   O  N N 355 
MPD   CM   C  N N 356 
MPD   C3   C  N N 357 
MPD   C4   C  N S 358 
MPD   O4   O  N N 359 
MPD   C5   C  N N 360 
MPD   H11  H  N N 361 
MPD   H12  H  N N 362 
MPD   H13  H  N N 363 
MPD   HO2  H  N N 364 
MPD   HM1  H  N N 365 
MPD   HM2  H  N N 366 
MPD   HM3  H  N N 367 
MPD   H31  H  N N 368 
MPD   H32  H  N N 369 
MPD   H4   H  N N 370 
MPD   HO4  H  N N 371 
MPD   H51  H  N N 372 
MPD   H52  H  N N 373 
MPD   H53  H  N N 374 
NAG   C1   C  N R 375 
NAG   C2   C  N R 376 
NAG   C3   C  N R 377 
NAG   C4   C  N S 378 
NAG   C5   C  N R 379 
NAG   C6   C  N N 380 
NAG   C7   C  N N 381 
NAG   C8   C  N N 382 
NAG   N2   N  N N 383 
NAG   O1   O  N N 384 
NAG   O3   O  N N 385 
NAG   O4   O  N N 386 
NAG   O5   O  N N 387 
NAG   O6   O  N N 388 
NAG   O7   O  N N 389 
NAG   H1   H  N N 390 
NAG   H2   H  N N 391 
NAG   H3   H  N N 392 
NAG   H4   H  N N 393 
NAG   H5   H  N N 394 
NAG   H61  H  N N 395 
NAG   H62  H  N N 396 
NAG   H81  H  N N 397 
NAG   H82  H  N N 398 
NAG   H83  H  N N 399 
NAG   HN2  H  N N 400 
NAG   HO1  H  N N 401 
NAG   HO3  H  N N 402 
NAG   HO4  H  N N 403 
NAG   HO6  H  N N 404 
PHE   N    N  N N 405 
PHE   CA   C  N S 406 
PHE   C    C  N N 407 
PHE   O    O  N N 408 
PHE   CB   C  N N 409 
PHE   CG   C  Y N 410 
PHE   CD1  C  Y N 411 
PHE   CD2  C  Y N 412 
PHE   CE1  C  Y N 413 
PHE   CE2  C  Y N 414 
PHE   CZ   C  Y N 415 
PHE   OXT  O  N N 416 
PHE   H    H  N N 417 
PHE   H2   H  N N 418 
PHE   HA   H  N N 419 
PHE   HB2  H  N N 420 
PHE   HB3  H  N N 421 
PHE   HD1  H  N N 422 
PHE   HD2  H  N N 423 
PHE   HE1  H  N N 424 
PHE   HE2  H  N N 425 
PHE   HZ   H  N N 426 
PHE   HXT  H  N N 427 
PRO   N    N  N N 428 
PRO   CA   C  N S 429 
PRO   C    C  N N 430 
PRO   O    O  N N 431 
PRO   CB   C  N N 432 
PRO   CG   C  N N 433 
PRO   CD   C  N N 434 
PRO   OXT  O  N N 435 
PRO   H    H  N N 436 
PRO   HA   H  N N 437 
PRO   HB2  H  N N 438 
PRO   HB3  H  N N 439 
PRO   HG2  H  N N 440 
PRO   HG3  H  N N 441 
PRO   HD2  H  N N 442 
PRO   HD3  H  N N 443 
PRO   HXT  H  N N 444 
SER   N    N  N N 445 
SER   CA   C  N S 446 
SER   C    C  N N 447 
SER   O    O  N N 448 
SER   CB   C  N N 449 
SER   OG   O  N N 450 
SER   OXT  O  N N 451 
SER   H    H  N N 452 
SER   H2   H  N N 453 
SER   HA   H  N N 454 
SER   HB2  H  N N 455 
SER   HB3  H  N N 456 
SER   HG   H  N N 457 
SER   HXT  H  N N 458 
THR   N    N  N N 459 
THR   CA   C  N S 460 
THR   C    C  N N 461 
THR   O    O  N N 462 
THR   CB   C  N R 463 
THR   OG1  O  N N 464 
THR   CG2  C  N N 465 
THR   OXT  O  N N 466 
THR   H    H  N N 467 
THR   H2   H  N N 468 
THR   HA   H  N N 469 
THR   HB   H  N N 470 
THR   HG1  H  N N 471 
THR   HG21 H  N N 472 
THR   HG22 H  N N 473 
THR   HG23 H  N N 474 
THR   HXT  H  N N 475 
TRP   N    N  N N 476 
TRP   CA   C  N S 477 
TRP   C    C  N N 478 
TRP   O    O  N N 479 
TRP   CB   C  N N 480 
TRP   CG   C  Y N 481 
TRP   CD1  C  Y N 482 
TRP   CD2  C  Y N 483 
TRP   NE1  N  Y N 484 
TRP   CE2  C  Y N 485 
TRP   CE3  C  Y N 486 
TRP   CZ2  C  Y N 487 
TRP   CZ3  C  Y N 488 
TRP   CH2  C  Y N 489 
TRP   OXT  O  N N 490 
TRP   H    H  N N 491 
TRP   H2   H  N N 492 
TRP   HA   H  N N 493 
TRP   HB2  H  N N 494 
TRP   HB3  H  N N 495 
TRP   HD1  H  N N 496 
TRP   HE1  H  N N 497 
TRP   HE3  H  N N 498 
TRP   HZ2  H  N N 499 
TRP   HZ3  H  N N 500 
TRP   HH2  H  N N 501 
TRP   HXT  H  N N 502 
TYR   N    N  N N 503 
TYR   CA   C  N S 504 
TYR   C    C  N N 505 
TYR   O    O  N N 506 
TYR   CB   C  N N 507 
TYR   CG   C  Y N 508 
TYR   CD1  C  Y N 509 
TYR   CD2  C  Y N 510 
TYR   CE1  C  Y N 511 
TYR   CE2  C  Y N 512 
TYR   CZ   C  Y N 513 
TYR   OH   O  N N 514 
TYR   OXT  O  N N 515 
TYR   H    H  N N 516 
TYR   H2   H  N N 517 
TYR   HA   H  N N 518 
TYR   HB2  H  N N 519 
TYR   HB3  H  N N 520 
TYR   HD1  H  N N 521 
TYR   HD2  H  N N 522 
TYR   HE1  H  N N 523 
TYR   HE2  H  N N 524 
TYR   HH   H  N N 525 
TYR   HXT  H  N N 526 
VAL   N    N  N N 527 
VAL   CA   C  N S 528 
VAL   C    C  N N 529 
VAL   O    O  N N 530 
VAL   CB   C  N N 531 
VAL   CG1  C  N N 532 
VAL   CG2  C  N N 533 
VAL   OXT  O  N N 534 
VAL   H    H  N N 535 
VAL   H2   H  N N 536 
VAL   HA   H  N N 537 
VAL   HB   H  N N 538 
VAL   HG11 H  N N 539 
VAL   HG12 H  N N 540 
VAL   HG13 H  N N 541 
VAL   HG21 H  N N 542 
VAL   HG22 H  N N 543 
VAL   HG23 H  N N 544 
VAL   HXT  H  N N 545 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1ATK CL1 C17  sing N N 1   
A1ATK C19 C17  doub Y N 2   
A1ATK C19 C20  sing Y N 3   
A1ATK C17 C15  sing Y N 4   
A1ATK C20 C13  doub Y N 5   
A1ATK C15 F16  sing N N 6   
A1ATK C15 C14  doub Y N 7   
A1ATK C13 C14  sing Y N 8   
A1ATK C13 N12  sing N N 9   
A1ATK N12 C10  sing N N 10  
A1ATK C10 O11  doub N N 11  
A1ATK C10 C09  sing N N 12  
A1ATK C21 C09  sing N N 13  
A1ATK C21 C22  sing N N 14  
A1ATK C09 C08  sing N N 15  
A1ATK C22 C23  sing N N 16  
A1ATK C08 N07  sing N N 17  
A1ATK C23 N07  sing N N 18  
A1ATK N07 C06  sing N N 19  
A1ATK C04 N05  sing N N 20  
A1ATK C04 C03  sing N N 21  
A1ATK C06 N05  sing N N 22  
A1ATK C06 O24  doub N N 23  
A1ATK N05 C25  sing N N 24  
A1ATK C03 N02  sing N N 25  
A1ATK C26 C25  sing N N 26  
A1ATK C26 N02  sing N N 27  
A1ATK N02 C01  sing N N 28  
A1ATK C01 O    doub N N 29  
A1ATK C01 CA   sing N N 30  
A1ATK CA  N    sing N N 31  
A1ATK CA  CB   sing N N 32  
A1ATK CB  CG   sing N N 33  
A1ATK CG  CD   sing N N 34  
A1ATK CD  NE   sing N N 35  
A1ATK NE  CZ   sing N N 36  
A1ATK CZ  NH1  doub N N 37  
A1ATK CZ  NH2  sing N N 38  
A1ATK N   H1   sing N N 39  
A1ATK N   H2   sing N N 40  
A1ATK CA  H4   sing N N 41  
A1ATK CB  H5   sing N N 42  
A1ATK CB  H6   sing N N 43  
A1ATK CG  H7   sing N N 44  
A1ATK CG  H8   sing N N 45  
A1ATK CD  H9   sing N N 46  
A1ATK CD  H10  sing N N 47  
A1ATK NE  H11  sing N N 48  
A1ATK NH1 H12  sing N N 49  
A1ATK NH2 H13  sing N N 50  
A1ATK NH2 H14  sing N N 51  
A1ATK C03 H15  sing N N 52  
A1ATK C03 H16  sing N N 53  
A1ATK C04 H17  sing N N 54  
A1ATK C04 H18  sing N N 55  
A1ATK C08 H19  sing N N 56  
A1ATK C08 H20  sing N N 57  
A1ATK C09 H21  sing N N 58  
A1ATK C14 H22  sing N N 59  
A1ATK C19 H23  sing N N 60  
A1ATK C20 H24  sing N N 61  
A1ATK C21 H25  sing N N 62  
A1ATK C21 H26  sing N N 63  
A1ATK C22 H27  sing N N 64  
A1ATK C22 H28  sing N N 65  
A1ATK C23 H29  sing N N 66  
A1ATK C23 H30  sing N N 67  
A1ATK C25 H31  sing N N 68  
A1ATK C25 H32  sing N N 69  
A1ATK C26 H33  sing N N 70  
A1ATK C26 H34  sing N N 71  
A1ATK N12 H35  sing N N 72  
ALA   N   CA   sing N N 73  
ALA   N   H    sing N N 74  
ALA   N   H2   sing N N 75  
ALA   CA  C    sing N N 76  
ALA   CA  CB   sing N N 77  
ALA   CA  HA   sing N N 78  
ALA   C   O    doub N N 79  
ALA   C   OXT  sing N N 80  
ALA   CB  HB1  sing N N 81  
ALA   CB  HB2  sing N N 82  
ALA   CB  HB3  sing N N 83  
ALA   OXT HXT  sing N N 84  
ARG   N   CA   sing N N 85  
ARG   N   H    sing N N 86  
ARG   N   H2   sing N N 87  
ARG   CA  C    sing N N 88  
ARG   CA  CB   sing N N 89  
ARG   CA  HA   sing N N 90  
ARG   C   O    doub N N 91  
ARG   C   OXT  sing N N 92  
ARG   CB  CG   sing N N 93  
ARG   CB  HB2  sing N N 94  
ARG   CB  HB3  sing N N 95  
ARG   CG  CD   sing N N 96  
ARG   CG  HG2  sing N N 97  
ARG   CG  HG3  sing N N 98  
ARG   CD  NE   sing N N 99  
ARG   CD  HD2  sing N N 100 
ARG   CD  HD3  sing N N 101 
ARG   NE  CZ   sing N N 102 
ARG   NE  HE   sing N N 103 
ARG   CZ  NH1  sing N N 104 
ARG   CZ  NH2  doub N N 105 
ARG   NH1 HH11 sing N N 106 
ARG   NH1 HH12 sing N N 107 
ARG   NH2 HH21 sing N N 108 
ARG   NH2 HH22 sing N N 109 
ARG   OXT HXT  sing N N 110 
ASN   N   CA   sing N N 111 
ASN   N   H    sing N N 112 
ASN   N   H2   sing N N 113 
ASN   CA  C    sing N N 114 
ASN   CA  CB   sing N N 115 
ASN   CA  HA   sing N N 116 
ASN   C   O    doub N N 117 
ASN   C   OXT  sing N N 118 
ASN   CB  CG   sing N N 119 
ASN   CB  HB2  sing N N 120 
ASN   CB  HB3  sing N N 121 
ASN   CG  OD1  doub N N 122 
ASN   CG  ND2  sing N N 123 
ASN   ND2 HD21 sing N N 124 
ASN   ND2 HD22 sing N N 125 
ASN   OXT HXT  sing N N 126 
ASP   N   CA   sing N N 127 
ASP   N   H    sing N N 128 
ASP   N   H2   sing N N 129 
ASP   CA  C    sing N N 130 
ASP   CA  CB   sing N N 131 
ASP   CA  HA   sing N N 132 
ASP   C   O    doub N N 133 
ASP   C   OXT  sing N N 134 
ASP   CB  CG   sing N N 135 
ASP   CB  HB2  sing N N 136 
ASP   CB  HB3  sing N N 137 
ASP   CG  OD1  doub N N 138 
ASP   CG  OD2  sing N N 139 
ASP   OD2 HD2  sing N N 140 
ASP   OXT HXT  sing N N 141 
CYS   N   CA   sing N N 142 
CYS   N   H    sing N N 143 
CYS   N   H2   sing N N 144 
CYS   CA  C    sing N N 145 
CYS   CA  CB   sing N N 146 
CYS   CA  HA   sing N N 147 
CYS   C   O    doub N N 148 
CYS   C   OXT  sing N N 149 
CYS   CB  SG   sing N N 150 
CYS   CB  HB2  sing N N 151 
CYS   CB  HB3  sing N N 152 
CYS   SG  HG   sing N N 153 
CYS   OXT HXT  sing N N 154 
EPE   N1  C2   sing N N 155 
EPE   N1  C6   sing N N 156 
EPE   N1  C9   sing N N 157 
EPE   C2  C3   sing N N 158 
EPE   C2  H21  sing N N 159 
EPE   C2  H22  sing N N 160 
EPE   C3  N4   sing N N 161 
EPE   C3  H31  sing N N 162 
EPE   C3  H32  sing N N 163 
EPE   N4  C5   sing N N 164 
EPE   N4  C7   sing N N 165 
EPE   C5  C6   sing N N 166 
EPE   C5  H51  sing N N 167 
EPE   C5  H52  sing N N 168 
EPE   C6  H61  sing N N 169 
EPE   C6  H62  sing N N 170 
EPE   C7  C8   sing N N 171 
EPE   C7  H71  sing N N 172 
EPE   C7  H72  sing N N 173 
EPE   C8  O8   sing N N 174 
EPE   C8  H81  sing N N 175 
EPE   C8  H82  sing N N 176 
EPE   O8  HO8  sing N N 177 
EPE   C9  C10  sing N N 178 
EPE   C9  H91  sing N N 179 
EPE   C9  H92  sing N N 180 
EPE   C10 S    sing N N 181 
EPE   C10 H101 sing N N 182 
EPE   C10 H102 sing N N 183 
EPE   S   O1S  doub N N 184 
EPE   S   O2S  doub N N 185 
EPE   S   O3S  sing N N 186 
EPE   O3S HOS3 sing N N 187 
GLN   N   CA   sing N N 188 
GLN   N   H    sing N N 189 
GLN   N   H2   sing N N 190 
GLN   CA  C    sing N N 191 
GLN   CA  CB   sing N N 192 
GLN   CA  HA   sing N N 193 
GLN   C   O    doub N N 194 
GLN   C   OXT  sing N N 195 
GLN   CB  CG   sing N N 196 
GLN   CB  HB2  sing N N 197 
GLN   CB  HB3  sing N N 198 
GLN   CG  CD   sing N N 199 
GLN   CG  HG2  sing N N 200 
GLN   CG  HG3  sing N N 201 
GLN   CD  OE1  doub N N 202 
GLN   CD  NE2  sing N N 203 
GLN   NE2 HE21 sing N N 204 
GLN   NE2 HE22 sing N N 205 
GLN   OXT HXT  sing N N 206 
GLU   N   CA   sing N N 207 
GLU   N   H    sing N N 208 
GLU   N   H2   sing N N 209 
GLU   CA  C    sing N N 210 
GLU   CA  CB   sing N N 211 
GLU   CA  HA   sing N N 212 
GLU   C   O    doub N N 213 
GLU   C   OXT  sing N N 214 
GLU   CB  CG   sing N N 215 
GLU   CB  HB2  sing N N 216 
GLU   CB  HB3  sing N N 217 
GLU   CG  CD   sing N N 218 
GLU   CG  HG2  sing N N 219 
GLU   CG  HG3  sing N N 220 
GLU   CD  OE1  doub N N 221 
GLU   CD  OE2  sing N N 222 
GLU   OE2 HE2  sing N N 223 
GLU   OXT HXT  sing N N 224 
GLY   N   CA   sing N N 225 
GLY   N   H    sing N N 226 
GLY   N   H2   sing N N 227 
GLY   CA  C    sing N N 228 
GLY   CA  HA2  sing N N 229 
GLY   CA  HA3  sing N N 230 
GLY   C   O    doub N N 231 
GLY   C   OXT  sing N N 232 
GLY   OXT HXT  sing N N 233 
HIS   N   CA   sing N N 234 
HIS   N   H    sing N N 235 
HIS   N   H2   sing N N 236 
HIS   CA  C    sing N N 237 
HIS   CA  CB   sing N N 238 
HIS   CA  HA   sing N N 239 
HIS   C   O    doub N N 240 
HIS   C   OXT  sing N N 241 
HIS   CB  CG   sing N N 242 
HIS   CB  HB2  sing N N 243 
HIS   CB  HB3  sing N N 244 
HIS   CG  ND1  sing Y N 245 
HIS   CG  CD2  doub Y N 246 
HIS   ND1 CE1  doub Y N 247 
HIS   ND1 HD1  sing N N 248 
HIS   CD2 NE2  sing Y N 249 
HIS   CD2 HD2  sing N N 250 
HIS   CE1 NE2  sing Y N 251 
HIS   CE1 HE1  sing N N 252 
HIS   NE2 HE2  sing N N 253 
HIS   OXT HXT  sing N N 254 
HOH   O   H1   sing N N 255 
HOH   O   H2   sing N N 256 
ILE   N   CA   sing N N 257 
ILE   N   H    sing N N 258 
ILE   N   H2   sing N N 259 
ILE   CA  C    sing N N 260 
ILE   CA  CB   sing N N 261 
ILE   CA  HA   sing N N 262 
ILE   C   O    doub N N 263 
ILE   C   OXT  sing N N 264 
ILE   CB  CG1  sing N N 265 
ILE   CB  CG2  sing N N 266 
ILE   CB  HB   sing N N 267 
ILE   CG1 CD1  sing N N 268 
ILE   CG1 HG12 sing N N 269 
ILE   CG1 HG13 sing N N 270 
ILE   CG2 HG21 sing N N 271 
ILE   CG2 HG22 sing N N 272 
ILE   CG2 HG23 sing N N 273 
ILE   CD1 HD11 sing N N 274 
ILE   CD1 HD12 sing N N 275 
ILE   CD1 HD13 sing N N 276 
ILE   OXT HXT  sing N N 277 
LEU   N   CA   sing N N 278 
LEU   N   H    sing N N 279 
LEU   N   H2   sing N N 280 
LEU   CA  C    sing N N 281 
LEU   CA  CB   sing N N 282 
LEU   CA  HA   sing N N 283 
LEU   C   O    doub N N 284 
LEU   C   OXT  sing N N 285 
LEU   CB  CG   sing N N 286 
LEU   CB  HB2  sing N N 287 
LEU   CB  HB3  sing N N 288 
LEU   CG  CD1  sing N N 289 
LEU   CG  CD2  sing N N 290 
LEU   CG  HG   sing N N 291 
LEU   CD1 HD11 sing N N 292 
LEU   CD1 HD12 sing N N 293 
LEU   CD1 HD13 sing N N 294 
LEU   CD2 HD21 sing N N 295 
LEU   CD2 HD22 sing N N 296 
LEU   CD2 HD23 sing N N 297 
LEU   OXT HXT  sing N N 298 
LYS   N   CA   sing N N 299 
LYS   N   H    sing N N 300 
LYS   N   H2   sing N N 301 
LYS   CA  C    sing N N 302 
LYS   CA  CB   sing N N 303 
LYS   CA  HA   sing N N 304 
LYS   C   O    doub N N 305 
LYS   C   OXT  sing N N 306 
LYS   CB  CG   sing N N 307 
LYS   CB  HB2  sing N N 308 
LYS   CB  HB3  sing N N 309 
LYS   CG  CD   sing N N 310 
LYS   CG  HG2  sing N N 311 
LYS   CG  HG3  sing N N 312 
LYS   CD  CE   sing N N 313 
LYS   CD  HD2  sing N N 314 
LYS   CD  HD3  sing N N 315 
LYS   CE  NZ   sing N N 316 
LYS   CE  HE2  sing N N 317 
LYS   CE  HE3  sing N N 318 
LYS   NZ  HZ1  sing N N 319 
LYS   NZ  HZ2  sing N N 320 
LYS   NZ  HZ3  sing N N 321 
LYS   OXT HXT  sing N N 322 
MET   N   CA   sing N N 323 
MET   N   H    sing N N 324 
MET   N   H2   sing N N 325 
MET   CA  C    sing N N 326 
MET   CA  CB   sing N N 327 
MET   CA  HA   sing N N 328 
MET   C   O    doub N N 329 
MET   C   OXT  sing N N 330 
MET   CB  CG   sing N N 331 
MET   CB  HB2  sing N N 332 
MET   CB  HB3  sing N N 333 
MET   CG  SD   sing N N 334 
MET   CG  HG2  sing N N 335 
MET   CG  HG3  sing N N 336 
MET   SD  CE   sing N N 337 
MET   CE  HE1  sing N N 338 
MET   CE  HE2  sing N N 339 
MET   CE  HE3  sing N N 340 
MET   OXT HXT  sing N N 341 
MPD   C1  C2   sing N N 342 
MPD   C1  H11  sing N N 343 
MPD   C1  H12  sing N N 344 
MPD   C1  H13  sing N N 345 
MPD   C2  O2   sing N N 346 
MPD   C2  CM   sing N N 347 
MPD   C2  C3   sing N N 348 
MPD   O2  HO2  sing N N 349 
MPD   CM  HM1  sing N N 350 
MPD   CM  HM2  sing N N 351 
MPD   CM  HM3  sing N N 352 
MPD   C3  C4   sing N N 353 
MPD   C3  H31  sing N N 354 
MPD   C3  H32  sing N N 355 
MPD   C4  O4   sing N N 356 
MPD   C4  C5   sing N N 357 
MPD   C4  H4   sing N N 358 
MPD   O4  HO4  sing N N 359 
MPD   C5  H51  sing N N 360 
MPD   C5  H52  sing N N 361 
MPD   C5  H53  sing N N 362 
NAG   C1  C2   sing N N 363 
NAG   C1  O1   sing N N 364 
NAG   C1  O5   sing N N 365 
NAG   C1  H1   sing N N 366 
NAG   C2  C3   sing N N 367 
NAG   C2  N2   sing N N 368 
NAG   C2  H2   sing N N 369 
NAG   C3  C4   sing N N 370 
NAG   C3  O3   sing N N 371 
NAG   C3  H3   sing N N 372 
NAG   C4  C5   sing N N 373 
NAG   C4  O4   sing N N 374 
NAG   C4  H4   sing N N 375 
NAG   C5  C6   sing N N 376 
NAG   C5  O5   sing N N 377 
NAG   C5  H5   sing N N 378 
NAG   C6  O6   sing N N 379 
NAG   C6  H61  sing N N 380 
NAG   C6  H62  sing N N 381 
NAG   C7  C8   sing N N 382 
NAG   C7  N2   sing N N 383 
NAG   C7  O7   doub N N 384 
NAG   C8  H81  sing N N 385 
NAG   C8  H82  sing N N 386 
NAG   C8  H83  sing N N 387 
NAG   N2  HN2  sing N N 388 
NAG   O1  HO1  sing N N 389 
NAG   O3  HO3  sing N N 390 
NAG   O4  HO4  sing N N 391 
NAG   O6  HO6  sing N N 392 
PHE   N   CA   sing N N 393 
PHE   N   H    sing N N 394 
PHE   N   H2   sing N N 395 
PHE   CA  C    sing N N 396 
PHE   CA  CB   sing N N 397 
PHE   CA  HA   sing N N 398 
PHE   C   O    doub N N 399 
PHE   C   OXT  sing N N 400 
PHE   CB  CG   sing N N 401 
PHE   CB  HB2  sing N N 402 
PHE   CB  HB3  sing N N 403 
PHE   CG  CD1  doub Y N 404 
PHE   CG  CD2  sing Y N 405 
PHE   CD1 CE1  sing Y N 406 
PHE   CD1 HD1  sing N N 407 
PHE   CD2 CE2  doub Y N 408 
PHE   CD2 HD2  sing N N 409 
PHE   CE1 CZ   doub Y N 410 
PHE   CE1 HE1  sing N N 411 
PHE   CE2 CZ   sing Y N 412 
PHE   CE2 HE2  sing N N 413 
PHE   CZ  HZ   sing N N 414 
PHE   OXT HXT  sing N N 415 
PRO   N   CA   sing N N 416 
PRO   N   CD   sing N N 417 
PRO   N   H    sing N N 418 
PRO   CA  C    sing N N 419 
PRO   CA  CB   sing N N 420 
PRO   CA  HA   sing N N 421 
PRO   C   O    doub N N 422 
PRO   C   OXT  sing N N 423 
PRO   CB  CG   sing N N 424 
PRO   CB  HB2  sing N N 425 
PRO   CB  HB3  sing N N 426 
PRO   CG  CD   sing N N 427 
PRO   CG  HG2  sing N N 428 
PRO   CG  HG3  sing N N 429 
PRO   CD  HD2  sing N N 430 
PRO   CD  HD3  sing N N 431 
PRO   OXT HXT  sing N N 432 
SER   N   CA   sing N N 433 
SER   N   H    sing N N 434 
SER   N   H2   sing N N 435 
SER   CA  C    sing N N 436 
SER   CA  CB   sing N N 437 
SER   CA  HA   sing N N 438 
SER   C   O    doub N N 439 
SER   C   OXT  sing N N 440 
SER   CB  OG   sing N N 441 
SER   CB  HB2  sing N N 442 
SER   CB  HB3  sing N N 443 
SER   OG  HG   sing N N 444 
SER   OXT HXT  sing N N 445 
THR   N   CA   sing N N 446 
THR   N   H    sing N N 447 
THR   N   H2   sing N N 448 
THR   CA  C    sing N N 449 
THR   CA  CB   sing N N 450 
THR   CA  HA   sing N N 451 
THR   C   O    doub N N 452 
THR   C   OXT  sing N N 453 
THR   CB  OG1  sing N N 454 
THR   CB  CG2  sing N N 455 
THR   CB  HB   sing N N 456 
THR   OG1 HG1  sing N N 457 
THR   CG2 HG21 sing N N 458 
THR   CG2 HG22 sing N N 459 
THR   CG2 HG23 sing N N 460 
THR   OXT HXT  sing N N 461 
TRP   N   CA   sing N N 462 
TRP   N   H    sing N N 463 
TRP   N   H2   sing N N 464 
TRP   CA  C    sing N N 465 
TRP   CA  CB   sing N N 466 
TRP   CA  HA   sing N N 467 
TRP   C   O    doub N N 468 
TRP   C   OXT  sing N N 469 
TRP   CB  CG   sing N N 470 
TRP   CB  HB2  sing N N 471 
TRP   CB  HB3  sing N N 472 
TRP   CG  CD1  doub Y N 473 
TRP   CG  CD2  sing Y N 474 
TRP   CD1 NE1  sing Y N 475 
TRP   CD1 HD1  sing N N 476 
TRP   CD2 CE2  doub Y N 477 
TRP   CD2 CE3  sing Y N 478 
TRP   NE1 CE2  sing Y N 479 
TRP   NE1 HE1  sing N N 480 
TRP   CE2 CZ2  sing Y N 481 
TRP   CE3 CZ3  doub Y N 482 
TRP   CE3 HE3  sing N N 483 
TRP   CZ2 CH2  doub Y N 484 
TRP   CZ2 HZ2  sing N N 485 
TRP   CZ3 CH2  sing Y N 486 
TRP   CZ3 HZ3  sing N N 487 
TRP   CH2 HH2  sing N N 488 
TRP   OXT HXT  sing N N 489 
TYR   N   CA   sing N N 490 
TYR   N   H    sing N N 491 
TYR   N   H2   sing N N 492 
TYR   CA  C    sing N N 493 
TYR   CA  CB   sing N N 494 
TYR   CA  HA   sing N N 495 
TYR   C   O    doub N N 496 
TYR   C   OXT  sing N N 497 
TYR   CB  CG   sing N N 498 
TYR   CB  HB2  sing N N 499 
TYR   CB  HB3  sing N N 500 
TYR   CG  CD1  doub Y N 501 
TYR   CG  CD2  sing Y N 502 
TYR   CD1 CE1  sing Y N 503 
TYR   CD1 HD1  sing N N 504 
TYR   CD2 CE2  doub Y N 505 
TYR   CD2 HD2  sing N N 506 
TYR   CE1 CZ   doub Y N 507 
TYR   CE1 HE1  sing N N 508 
TYR   CE2 CZ   sing Y N 509 
TYR   CE2 HE2  sing N N 510 
TYR   CZ  OH   sing N N 511 
TYR   OH  HH   sing N N 512 
TYR   OXT HXT  sing N N 513 
VAL   N   CA   sing N N 514 
VAL   N   H    sing N N 515 
VAL   N   H2   sing N N 516 
VAL   CA  C    sing N N 517 
VAL   CA  CB   sing N N 518 
VAL   CA  HA   sing N N 519 
VAL   C   O    doub N N 520 
VAL   C   OXT  sing N N 521 
VAL   CB  CG1  sing N N 522 
VAL   CB  CG2  sing N N 523 
VAL   CB  HB   sing N N 524 
VAL   CG1 HG11 sing N N 525 
VAL   CG1 HG12 sing N N 526 
VAL   CG1 HG13 sing N N 527 
VAL   CG2 HG21 sing N N 528 
VAL   CG2 HG22 sing N N 529 
VAL   CG2 HG23 sing N N 530 
VAL   OXT HXT  sing N N 531 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 'R01 AI174908' 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 'P01 AI162242' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6ONF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BXD 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016390 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015189 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011048 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL   A 1 3   ? -24.048 -14.761 0.442   1.00 53.29  ? 44  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 3   ? -23.281 -14.184 1.536   1.00 53.26  ? 44  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 3   ? -21.968 -13.644 0.985   1.00 54.94  ? 44  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 3   ? -21.349 -14.258 0.115   1.00 55.85  ? 44  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 3   ? -23.046 -15.216 2.657   1.00 56.98  ? 44  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 3   ? -22.137 -14.644 3.746   1.00 60.28  ? 44  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 3   ? -24.381 -15.655 3.247   1.00 50.97  ? 44  VAL   A CG2 1 
ATOM   8    N  N   . TRP   A 1 4   ? -21.548 -12.489 1.493   1.00 55.17  ? 45  TRP   A N   1 
ATOM   9    C  CA  . TRP   A 1 4   ? -20.412 -11.781 0.927   1.00 54.79  ? 45  TRP   A CA  1 
ATOM   10   C  C   . TRP   A 1 4   ? -19.817 -10.880 1.996   1.00 55.34  ? 45  TRP   A C   1 
ATOM   11   O  O   . TRP   A 1 4   ? -20.441 -10.618 3.027   1.00 58.50  ? 45  TRP   A O   1 
ATOM   12   C  CB  . TRP   A 1 4   ? -20.848 -10.958 -0.292  1.00 53.29  ? 45  TRP   A CB  1 
ATOM   13   C  CG  . TRP   A 1 4   ? -21.627 -9.744  0.097   1.00 52.26  ? 45  TRP   A CG  1 
ATOM   14   C  CD1 . TRP   A 1 4   ? -21.135 -8.569  0.594   1.00 52.48  ? 45  TRP   A CD1 1 
ATOM   15   C  CD2 . TRP   A 1 4   ? -23.049 -9.630  0.142   1.00 51.45  ? 45  TRP   A CD2 1 
ATOM   16   N  NE1 . TRP   A 1 4   ? -22.163 -7.708  0.881   1.00 51.84  ? 45  TRP   A NE1 1 
ATOM   17   C  CE2 . TRP   A 1 4   ? -23.351 -8.340  0.617   1.00 53.45  ? 45  TRP   A CE2 1 
ATOM   18   C  CE3 . TRP   A 1 4   ? -24.101 -10.485 -0.203  1.00 52.45  ? 45  TRP   A CE3 1 
ATOM   19   C  CZ2 . TRP   A 1 4   ? -24.657 -7.886  0.755   1.00 54.67  ? 45  TRP   A CZ2 1 
ATOM   20   C  CZ3 . TRP   A 1 4   ? -25.393 -10.030 -0.066  1.00 56.89  ? 45  TRP   A CZ3 1 
ATOM   21   C  CH2 . TRP   A 1 4   ? -25.661 -8.745  0.409   1.00 53.38  ? 45  TRP   A CH2 1 
ATOM   22   N  N   . LYS   A 1 5   ? -18.612 -10.387 1.723   1.00 54.03  ? 46  LYS   A N   1 
ATOM   23   C  CA  . LYS   A 1 5   ? -17.981 -9.382  2.566   1.00 52.40  ? 46  LYS   A CA  1 
ATOM   24   C  C   . LYS   A 1 5   ? -17.198 -8.414  1.692   1.00 52.19  ? 46  LYS   A C   1 
ATOM   25   O  O   . LYS   A 1 5   ? -16.866 -8.710  0.541   1.00 47.77  ? 46  LYS   A O   1 
ATOM   26   C  CB  . LYS   A 1 5   ? -17.061 -10.007 3.627   1.00 54.43  ? 46  LYS   A CB  1 
ATOM   27   C  CG  . LYS   A 1 5   ? -15.744 -10.552 3.097   1.00 56.49  ? 46  LYS   A CG  1 
ATOM   28   C  CD  . LYS   A 1 5   ? -15.114 -11.497 4.114   1.00 55.67  ? 46  LYS   A CD  1 
ATOM   29   C  CE  . LYS   A 1 5   ? -13.987 -12.320 3.508   1.00 60.41  ? 46  LYS   A CE  1 
ATOM   30   N  NZ  . LYS   A 1 5   ? -13.087 -12.905 4.549   1.00 64.21  ? 46  LYS   A NZ  1 
ATOM   31   N  N   . ASP   A 1 6   ? -16.926 -7.237  2.252   1.00 52.28  ? 47  ASP   A N   1 
ATOM   32   C  CA  . ASP   A 1 6   ? -16.119 -6.242  1.556   1.00 52.67  ? 47  ASP   A CA  1 
ATOM   33   C  C   . ASP   A 1 6   ? -14.728 -6.792  1.286   1.00 55.84  ? 47  ASP   A C   1 
ATOM   34   O  O   . ASP   A 1 6   ? -14.009 -7.177  2.214   1.00 57.45  ? 47  ASP   A O   1 
ATOM   35   C  CB  . ASP   A 1 6   ? -16.037 -4.946  2.359   1.00 51.29  ? 47  ASP   A CB  1 
ATOM   36   C  CG  . ASP   A 1 6   ? -17.215 -4.051  2.108   1.00 53.70  ? 47  ASP   A CG  1 
ATOM   37   O  OD1 . ASP   A 1 6   ? -17.777 -4.176  1.009   1.00 56.00  ? 47  ASP   A OD1 1 
ATOM   38   O  OD2 . ASP   A 1 6   ? -17.562 -3.204  2.958   1.00 58.36  ? 47  ASP   A OD2 1 
ATOM   39   N  N   . ALA   A 1 7   ? -14.343 -6.823  0.015   1.00 49.58  ? 48  ALA   A N   1 
ATOM   40   C  CA  . ALA   A 1 7   ? -13.022 -7.308  -0.336  1.00 50.79  ? 48  ALA   A CA  1 
ATOM   41   C  C   . ALA   A 1 7   ? -12.511 -6.574  -1.565  1.00 49.05  ? 48  ALA   A C   1 
ATOM   42   O  O   . ALA   A 1 7   ? -13.267 -5.944  -2.310  1.00 46.22  ? 48  ALA   A O   1 
ATOM   43   C  CB  . ALA   A 1 7   ? -13.017 -8.823  -0.582  1.00 51.14  ? 48  ALA   A CB  1 
ATOM   44   N  N   . ASP   A 1 8   ? -11.204 -6.686  -1.764  1.00 49.88  ? 49  ASP   A N   1 
ATOM   45   C  CA  . ASP   A 1 8   ? -10.510 -6.164  -2.926  1.00 46.41  ? 49  ASP   A CA  1 
ATOM   46   C  C   . ASP   A 1 8   ? -9.835  -7.332  -3.626  1.00 48.11  ? 49  ASP   A C   1 
ATOM   47   O  O   . ASP   A 1 8   ? -9.214  -8.178  -2.977  1.00 47.59  ? 49  ASP   A O   1 
ATOM   48   C  CB  . ASP   A 1 8   ? -9.456  -5.120  -2.527  1.00 44.53  ? 49  ASP   A CB  1 
ATOM   49   C  CG  . ASP   A 1 8   ? -10.065 -3.812  -2.052  1.00 44.24  ? 49  ASP   A CG  1 
ATOM   50   O  OD1 . ASP   A 1 8   ? -11.286 -3.604  -2.225  1.00 41.74  ? 49  ASP   A OD1 1 
ATOM   51   O  OD2 . ASP   A 1 8   ? -9.315  -2.986  -1.487  1.00 43.58  ? 49  ASP   A OD2 1 
ATOM   52   N  N   . THR   A 1 9   ? -9.972  -7.399  -4.945  1.00 46.54  ? 50  THR   A N   1 
ATOM   53   C  CA  . THR   A 1 9   ? -9.275  -8.413  -5.720  1.00 42.20  ? 50  THR   A CA  1 
ATOM   54   C  C   . THR   A 1 9   ? -8.799  -7.779  -7.015  1.00 41.53  ? 50  THR   A C   1 
ATOM   55   O  O   . THR   A 1 9   ? -9.026  -6.594  -7.267  1.00 45.34  ? 50  THR   A O   1 
ATOM   56   C  CB  . THR   A 1 9   ? -10.158 -9.638  -5.980  1.00 43.59  ? 50  THR   A CB  1 
ATOM   57   O  OG1 . THR   A 1 9   ? -9.343  -10.698 -6.494  1.00 47.67  ? 50  THR   A OG1 1 
ATOM   58   C  CG2 . THR   A 1 9   ? -11.246 -9.307  -6.977  1.00 44.92  ? 50  THR   A CG2 1 
ATOM   59   N  N   . THR   A 1 10  ? -8.104  -8.559  -7.831  1.00 38.32  ? 51  THR   A N   1 
ATOM   60   C  CA  . THR   A 1 10  ? -7.644  -8.073  -9.122  1.00 40.78  ? 51  THR   A CA  1 
ATOM   61   C  C   . THR   A 1 10  ? -8.772  -8.214  -10.133 1.00 41.47  ? 51  THR   A C   1 
ATOM   62   O  O   . THR   A 1 10  ? -9.243  -9.326  -10.394 1.00 42.51  ? 51  THR   A O   1 
ATOM   63   C  CB  . THR   A 1 10  ? -6.415  -8.836  -9.604  1.00 40.87  ? 51  THR   A CB  1 
ATOM   64   O  OG1 . THR   A 1 10  ? -5.348  -8.670  -8.663  1.00 42.22  ? 51  THR   A OG1 1 
ATOM   65   C  CG2 . THR   A 1 10  ? -5.981  -8.290  -10.938 1.00 49.25  ? 51  THR   A CG2 1 
ATOM   66   N  N   . LEU   A 1 11  ? -9.198  -7.093  -10.696 1.00 37.27  ? 52  LEU   A N   1 
ATOM   67   C  CA  . LEU   A 1 11  ? -10.241 -7.081  -11.702 1.00 34.93  ? 52  LEU   A CA  1 
ATOM   68   C  C   . LEU   A 1 11  ? -9.634  -7.342  -13.073 1.00 33.00  ? 52  LEU   A C   1 
ATOM   69   O  O   . LEU   A 1 11  ? -8.427  -7.214  -13.281 1.00 34.90  ? 52  LEU   A O   1 
ATOM   70   C  CB  . LEU   A 1 11  ? -10.969 -5.731  -11.686 1.00 35.48  ? 52  LEU   A CB  1 
ATOM   71   C  CG  . LEU   A 1 11  ? -11.633 -5.355  -10.359 1.00 39.18  ? 52  LEU   A CG  1 
ATOM   72   C  CD1 . LEU   A 1 11  ? -12.040 -3.885  -10.336 1.00 36.79  ? 52  LEU   A CD1 1 
ATOM   73   C  CD2 . LEU   A 1 11  ? -12.823 -6.250  -10.087 1.00 40.50  ? 52  LEU   A CD2 1 
ATOM   74   N  N   . PHE   A 1 12  ? -10.489 -7.715  -14.015 1.00 35.98  ? 53  PHE   A N   1 
ATOM   75   C  CA  . PHE   A 1 12  ? -10.141 -7.734  -15.426 1.00 35.74  ? 53  PHE   A CA  1 
ATOM   76   C  C   . PHE   A 1 12  ? -11.122 -6.844  -16.175 1.00 34.96  ? 53  PHE   A C   1 
ATOM   77   O  O   . PHE   A 1 12  ? -12.145 -6.422  -15.631 1.00 33.83  ? 53  PHE   A O   1 
ATOM   78   C  CB  . PHE   A 1 12  ? -10.106 -9.165  -15.987 1.00 32.66  ? 53  PHE   A CB  1 
ATOM   79   C  CG  . PHE   A 1 12  ? -11.457 -9.834  -16.115 1.00 37.57  ? 53  PHE   A CG  1 
ATOM   80   C  CD1 . PHE   A 1 12  ? -11.992 -10.559 -15.061 1.00 36.04  ? 53  PHE   A CD1 1 
ATOM   81   C  CD2 . PHE   A 1 12  ? -12.165 -9.786  -17.306 1.00 34.64  ? 53  PHE   A CD2 1 
ATOM   82   C  CE1 . PHE   A 1 12  ? -13.214 -11.197 -15.185 1.00 38.18  ? 53  PHE   A CE1 1 
ATOM   83   C  CE2 . PHE   A 1 12  ? -13.387 -10.418 -17.429 1.00 37.08  ? 53  PHE   A CE2 1 
ATOM   84   C  CZ  . PHE   A 1 12  ? -13.907 -11.127 -16.370 1.00 37.26  ? 53  PHE   A CZ  1 
ATOM   85   N  N   . CYS   A 1 13  ? -10.785 -6.508  -17.417 1.00 32.01  ? 54  CYS   A N   1 
ATOM   86   C  CA  . CYS   A 1 13  ? -11.619 -5.594  -18.176 1.00 30.93  ? 54  CYS   A CA  1 
ATOM   87   C  C   . CYS   A 1 13  ? -12.219 -6.304  -19.377 1.00 30.31  ? 54  CYS   A C   1 
ATOM   88   O  O   . CYS   A 1 13  ? -11.704 -7.317  -19.861 1.00 32.84  ? 54  CYS   A O   1 
ATOM   89   C  CB  . CYS   A 1 13  ? -10.855 -4.355  -18.669 1.00 28.81  ? 54  CYS   A CB  1 
ATOM   90   S  SG  . CYS   A 1 13  ? -9.317  -4.678  -19.523 1.00 34.88  ? 54  CYS   A SG  1 
ATOM   91   N  N   . ALA   A 1 14  ? -13.321 -5.738  -19.854 1.00 32.28  ? 55  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 14  ? -13.996 -6.207  -21.049 1.00 34.01  ? 55  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 14  ? -14.363 -5.004  -21.900 1.00 35.56  ? 55  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 14  ? -14.658 -3.923  -21.379 1.00 35.93  ? 55  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 14  ? -15.247 -7.022  -20.708 1.00 37.51  ? 55  ALA   A CB  1 
ATOM   96   N  N   . SER   A 1 15  ? -14.349 -5.198  -23.214 1.00 39.06  ? 56  SER   A N   1 
ATOM   97   C  CA  . SER   A 1 15  ? -14.610 -4.097  -24.129 1.00 40.20  ? 56  SER   A CA  1 
ATOM   98   C  C   . SER   A 1 15  ? -15.105 -4.664  -25.451 1.00 42.36  ? 56  SER   A C   1 
ATOM   99   O  O   . SER   A 1 15  ? -14.907 -5.841  -25.765 1.00 41.42  ? 56  SER   A O   1 
ATOM   100  C  CB  . SER   A 1 15  ? -13.363 -3.242  -24.357 1.00 39.24  ? 56  SER   A CB  1 
ATOM   101  O  OG  . SER   A 1 15  ? -12.575 -3.822  -25.377 1.00 43.95  ? 56  SER   A OG  1 
ATOM   102  N  N   . ASP   A 1 16  ? -15.760 -3.801  -26.226 1.00 39.11  ? 57  ASP   A N   1 
ATOM   103  C  CA  . ASP   A 1 16  ? -16.173 -4.110  -27.587 1.00 41.23  ? 57  ASP   A CA  1 
ATOM   104  C  C   . ASP   A 1 16  ? -15.157 -3.618  -28.612 1.00 44.78  ? 57  ASP   A C   1 
ATOM   105  O  O   . ASP   A 1 16  ? -15.529 -3.201  -29.716 1.00 43.41  ? 57  ASP   A O   1 
ATOM   106  C  CB  . ASP   A 1 16  ? -17.547 -3.510  -27.855 1.00 43.52  ? 57  ASP   A CB  1 
ATOM   107  C  CG  . ASP   A 1 16  ? -18.614 -4.105  -26.955 1.00 44.43  ? 57  ASP   A CG  1 
ATOM   108  O  OD1 . ASP   A 1 16  ? -18.565 -5.331  -26.710 1.00 51.08  ? 57  ASP   A OD1 1 
ATOM   109  O  OD2 . ASP   A 1 16  ? -19.490 -3.351  -26.475 1.00 51.16  ? 57  ASP   A OD2 1 
ATOM   110  N  N   . ALA   A 1 17  ? -13.876 -3.647  -28.247 1.00 42.06  ? 58  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 17  ? -12.815 -3.225  -29.148 1.00 41.83  ? 58  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 17  ? -12.843 -4.047  -30.428 1.00 46.33  ? 58  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 17  ? -13.057 -5.262  -30.406 1.00 45.15  ? 58  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 17  ? -11.457 -3.369  -28.466 1.00 43.45  ? 58  ALA   A CB  1 
ATOM   115  N  N   . LYS   A 1 18  ? -12.600 -3.379  -31.547 1.00 49.30  ? 59  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 18  ? -12.557 -4.031  -32.847 1.00 51.79  ? 59  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 18  ? -11.114 -4.430  -33.124 1.00 52.13  ? 59  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 18  ? -10.233 -3.569  -33.190 1.00 50.98  ? 59  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 18  ? -13.068 -3.092  -33.937 1.00 52.64  ? 59  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 18  ? -14.281 -2.271  -33.529 1.00 55.25  ? 59  LYS   A CG  1 
ATOM   121  C  CD  . LYS   A 1 18  ? -15.436 -3.121  -33.017 1.00 57.57  ? 59  LYS   A CD  1 
ATOM   122  C  CE  . LYS   A 1 18  ? -16.630 -2.232  -32.694 1.00 59.47  ? 59  LYS   A CE  1 
ATOM   123  N  NZ  . LYS   A 1 18  ? -17.566 -2.097  -33.840 1.00 58.43  ? 59  LYS   A NZ  1 
ATOM   124  N  N   . ALA   A 1 19  ? -10.865 -5.729  -33.275 1.00 54.01  ? 60  ALA   A N   1 
ATOM   125  C  CA  . ALA   A 1 19  ? -9.508  -6.209  -33.538 1.00 53.79  ? 60  ALA   A CA  1 
ATOM   126  C  C   . ALA   A 1 19  ? -9.159  -5.933  -34.999 1.00 60.63  ? 60  ALA   A C   1 
ATOM   127  O  O   . ALA   A 1 19  ? -9.036  -6.838  -35.827 1.00 66.18  ? 60  ALA   A O   1 
ATOM   128  C  CB  . ALA   A 1 19  ? -9.372  -7.688  -33.217 1.00 52.59  ? 60  ALA   A CB  1 
ATOM   129  N  N   . TYR   A 1 20  ? -9.029  -4.643  -35.305 1.00 51.53  ? 61  TYR   A N   1 
ATOM   130  C  CA  . TYR   A 1 20  ? -8.550  -4.167  -36.595 1.00 54.08  ? 61  TYR   A CA  1 
ATOM   131  C  C   . TYR   A 1 20  ? -8.167  -2.700  -36.440 1.00 53.92  ? 61  TYR   A C   1 
ATOM   132  O  O   . TYR   A 1 20  ? -7.222  -2.219  -37.072 1.00 48.92  ? 61  TYR   A O   1 
ATOM   133  C  CB  . TYR   A 1 20  ? -9.607  -4.421  -37.694 1.00 58.12  ? 61  TYR   A CB  1 
ATOM   134  C  CG  . TYR   A 1 20  ? -10.961 -3.696  -37.623 1.00 59.98  ? 61  TYR   A CG  1 
ATOM   135  C  CD1 . TYR   A 1 20  ? -11.056 -2.320  -37.461 1.00 60.33  ? 61  TYR   A CD1 1 
ATOM   136  C  CD2 . TYR   A 1 20  ? -12.147 -4.414  -37.684 1.00 59.95  ? 61  TYR   A CD2 1 
ATOM   137  C  CE1 . TYR   A 1 20  ? -12.272 -1.676  -37.389 1.00 62.59  ? 61  TYR   A CE1 1 
ATOM   138  C  CE2 . TYR   A 1 20  ? -13.379 -3.775  -37.615 1.00 64.62  ? 61  TYR   A CE2 1 
ATOM   139  C  CZ  . TYR   A 1 20  ? -13.433 -2.402  -37.465 1.00 68.79  ? 61  TYR   A CZ  1 
ATOM   140  O  OH  . TYR   A 1 20  ? -14.643 -1.738  -37.390 1.00 72.29  ? 61  TYR   A OH  1 
ATOM   141  N  N   . GLU   A 1 21  ? -8.849  -2.013  -35.528 1.00 51.45  ? 62  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 21  ? -8.773  -0.563  -35.454 1.00 43.37  ? 62  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 21  ? -7.429  -0.134  -34.884 1.00 42.43  ? 62  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 21  ? -6.915  -0.741  -33.943 1.00 43.75  ? 62  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 21  ? -9.922  -0.032  -34.594 1.00 45.34  ? 62  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 21  ? -9.923  1.459   -34.370 1.00 46.48  ? 62  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 21  ? -10.303 2.243   -35.608 1.00 48.58  ? 62  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 21  ? -11.511 2.319   -35.926 1.00 52.34  ? 62  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 21  ? -9.395  2.787   -36.273 1.00 46.82  ? 62  GLU   A OE2 1 
ATOM   150  N  N   . THR   A 1 22  ? -6.845  0.907   -35.469 1.00 43.31  ? 63  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 22  ? -5.606  1.439   -34.921 1.00 40.52  ? 63  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 22  ? -5.839  2.466   -33.822 1.00 37.04  ? 63  THR   A C   1 
ATOM   153  O  O   . THR   A 1 22  ? -4.871  2.901   -33.189 1.00 33.19  ? 63  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 22  ? -4.747  2.068   -36.024 1.00 43.21  ? 63  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 22  ? -5.515  3.050   -36.733 1.00 43.51  ? 63  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 22  ? -4.273  1.008   -37.001 1.00 41.08  ? 63  THR   A CG2 1 
ATOM   157  N  N   . GLU   A 1 23  ? -7.089  2.858   -33.581 1.00 38.70  ? 64  GLU   A N   1 
ATOM   158  C  CA  . GLU   A 1 23  ? -7.387  3.768   -32.488 1.00 33.15  ? 64  GLU   A CA  1 
ATOM   159  C  C   . GLU   A 1 23  ? -6.883  3.168   -31.183 1.00 35.04  ? 64  GLU   A C   1 
ATOM   160  O  O   . GLU   A 1 23  ? -7.100  1.987   -30.895 1.00 38.24  ? 64  GLU   A O   1 
ATOM   161  C  CB  . GLU   A 1 23  ? -8.886  4.059   -32.431 1.00 35.42  ? 64  GLU   A CB  1 
ATOM   162  C  CG  . GLU   A 1 23  ? -9.247  5.174   -31.490 1.00 36.96  ? 64  GLU   A CG  1 
ATOM   163  C  CD  . GLU   A 1 23  ? -9.114  4.769   -30.064 1.00 36.32  ? 64  GLU   A CD  1 
ATOM   164  O  OE1 . GLU   A 1 23  ? -9.440  3.609   -29.712 1.00 34.22  ? 64  GLU   A OE1 1 
ATOM   165  O  OE2 . GLU   A 1 23  ? -8.691  5.616   -29.243 1.00 29.81  ? 64  GLU   A OE2 1 
ATOM   166  N  N   . VAL   A 1 24  ? -6.222  4.007   -30.387 1.00 28.24  ? 65  VAL   A N   1 
ATOM   167  C  CA  . VAL   A 1 24  ? -5.337  3.509   -29.341 1.00 30.72  ? 65  VAL   A CA  1 
ATOM   168  C  C   . VAL   A 1 24  ? -6.097  2.773   -28.239 1.00 28.24  ? 65  VAL   A C   1 
ATOM   169  O  O   . VAL   A 1 24  ? -5.586  1.796   -27.679 1.00 31.77  ? 65  VAL   A O   1 
ATOM   170  C  CB  . VAL   A 1 24  ? -4.487  4.663   -28.789 1.00 27.71  ? 65  VAL   A CB  1 
ATOM   171  C  CG1 . VAL   A 1 24  ? -3.577  5.189   -29.871 1.00 31.78  ? 65  VAL   A CG1 1 
ATOM   172  C  CG2 . VAL   A 1 24  ? -5.376  5.785   -28.277 1.00 27.35  ? 65  VAL   A CG2 1 
ATOM   173  N  N   . HIS   A 1 25  ? -7.308  3.223   -27.886 1.00 29.22  ? 66  HIS   A N   1 
ATOM   174  C  CA  . HIS   A 1 25  ? -8.039  2.499   -26.844 1.00 32.06  ? 66  HIS   A CA  1 
ATOM   175  C  C   . HIS   A 1 25  ? -8.533  1.155   -27.372 1.00 30.88  ? 66  HIS   A C   1 
ATOM   176  O  O   . HIS   A 1 25  ? -8.621  0.179   -26.615 1.00 29.15  ? 66  HIS   A O   1 
ATOM   177  C  CB  . HIS   A 1 25  ? -9.221  3.317   -26.317 1.00 30.93  ? 66  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A 1 25  ? -8.847  4.613   -25.655 1.00 30.67  ? 66  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A 1 25  ? -8.538  5.743   -26.380 1.00 29.99  ? 66  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A 1 25  ? -8.889  5.009   -24.361 1.00 30.95  ? 66  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A 1 25  ? -8.310  6.752   -25.557 1.00 29.96  ? 66  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A 1 25  ? -8.524  6.335   -24.324 1.00 34.65  ? 66  HIS   A NE2 1 
ATOM   183  N  N   . ASN   A 1 26  ? -8.875  1.088   -28.666 1.00 34.33  ? 67  ASN   A N   1 
ATOM   184  C  CA  . ASN   A 1 26  ? -9.235  -0.195  -29.265 1.00 34.60  ? 67  ASN   A CA  1 
ATOM   185  C  C   . ASN   A 1 26  ? -8.056  -1.154  -29.250 1.00 37.88  ? 67  ASN   A C   1 
ATOM   186  O  O   . ASN   A 1 26  ? -8.203  -2.329  -28.891 1.00 34.15  ? 67  ASN   A O   1 
ATOM   187  C  CB  . ASN   A 1 26  ? -9.755  -0.013  -30.693 1.00 35.09  ? 67  ASN   A CB  1 
ATOM   188  C  CG  . ASN   A 1 26  ? -11.171 0.517   -30.736 1.00 41.57  ? 67  ASN   A CG  1 
ATOM   189  O  OD1 . ASN   A 1 26  ? -12.135 -0.254  -30.774 1.00 38.12  ? 67  ASN   A OD1 1 
ATOM   190  N  ND2 . ASN   A 1 26  ? -11.307 1.836   -30.737 1.00 34.68  ? 67  ASN   A ND2 1 
ATOM   191  N  N   . VAL   A 1 27  ? -6.871  -0.665  -29.624 1.00 31.51  ? 68  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 27  ? -5.681  -1.511  -29.626 1.00 34.62  ? 68  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 27  ? -5.371  -1.995  -28.217 1.00 34.52  ? 68  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 27  ? -5.069  -3.177  -28.001 1.00 32.01  ? 68  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 27  ? -4.485  -0.756  -30.237 1.00 36.11  ? 68  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 27  ? -3.181  -1.460  -29.898 1.00 31.17  ? 68  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 27  ? -4.650  -0.624  -31.740 1.00 37.11  ? 68  VAL   A CG2 1 
ATOM   198  N  N   . TRP   A 1 28  ? -5.450  -1.094  -27.235 1.00 32.04  ? 69  TRP   A N   1 
ATOM   199  C  CA  . TRP   A 1 28  ? -5.184  -1.480  -25.853 1.00 31.83  ? 69  TRP   A CA  1 
ATOM   200  C  C   . TRP   A 1 28  ? -6.228  -2.465  -25.345 1.00 31.66  ? 69  TRP   A C   1 
ATOM   201  O  O   . TRP   A 1 28  ? -5.888  -3.490  -24.742 1.00 33.49  ? 69  TRP   A O   1 
ATOM   202  C  CB  . TRP   A 1 28  ? -5.139  -0.243  -24.959 1.00 30.51  ? 69  TRP   A CB  1 
ATOM   203  C  CG  . TRP   A 1 28  ? -4.930  -0.579  -23.516 1.00 25.51  ? 69  TRP   A CG  1 
ATOM   204  C  CD1 . TRP   A 1 28  ? -3.735  -0.724  -22.877 1.00 28.27  ? 69  TRP   A CD1 1 
ATOM   205  C  CD2 . TRP   A 1 28  ? -5.943  -0.796  -22.528 1.00 26.47  ? 69  TRP   A CD2 1 
ATOM   206  N  NE1 . TRP   A 1 28  ? -3.939  -1.028  -21.553 1.00 33.14  ? 69  TRP   A NE1 1 
ATOM   207  C  CE2 . TRP   A 1 28  ? -5.287  -1.077  -21.314 1.00 27.19  ? 69  TRP   A CE2 1 
ATOM   208  C  CE3 . TRP   A 1 28  ? -7.340  -0.783  -22.553 1.00 27.23  ? 69  TRP   A CE3 1 
ATOM   209  C  CZ2 . TRP   A 1 28  ? -5.980  -1.341  -20.136 1.00 23.44  ? 69  TRP   A CZ2 1 
ATOM   210  C  CZ3 . TRP   A 1 28  ? -8.026  -1.045  -21.384 1.00 28.33  ? 69  TRP   A CZ3 1 
ATOM   211  C  CH2 . TRP   A 1 28  ? -7.345  -1.322  -20.192 1.00 26.72  ? 69  TRP   A CH2 1 
ATOM   212  N  N   . ALA   A 1 29  ? -7.508  -2.174  -25.589 1.00 29.82  ? 70  ALA   A N   1 
ATOM   213  C  CA  . ALA   A 1 29  ? -8.567  -3.063  -25.129 1.00 32.49  ? 70  ALA   A CA  1 
ATOM   214  C  C   . ALA   A 1 29  ? -8.505  -4.416  -25.828 1.00 32.63  ? 70  ALA   A C   1 
ATOM   215  O  O   . ALA   A 1 29  ? -8.926  -5.431  -25.256 1.00 35.81  ? 70  ALA   A O   1 
ATOM   216  C  CB  . ALA   A 1 29  ? -9.925  -2.405  -25.341 1.00 30.41  ? 70  ALA   A CB  1 
ATOM   217  N  N   . THR   A 1 30  ? -7.982  -4.454  -27.059 1.00 35.01  ? 71  THR   A N   1 
ATOM   218  C  CA  . THR   A 1 30  ? -7.918  -5.711  -27.798 1.00 34.81  ? 71  THR   A CA  1 
ATOM   219  C  C   . THR   A 1 30  ? -6.981  -6.708  -27.121 1.00 32.27  ? 71  THR   A C   1 
ATOM   220  O  O   . THR   A 1 30  ? -7.263  -7.914  -27.093 1.00 39.37  ? 71  THR   A O   1 
ATOM   221  C  CB  . THR   A 1 30  ? -7.486  -5.451  -29.243 1.00 36.73  ? 71  THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 30  ? -8.575  -4.877  -29.976 1.00 34.63  ? 71  THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 30  ? -7.073  -6.751  -29.929 1.00 38.89  ? 71  THR   A CG2 1 
ATOM   224  N  N   . HIS   A 1 31  ? -5.872  -6.226  -26.549 1.00 29.56  ? 72  HIS   A N   1 
ATOM   225  C  CA  . HIS   A 1 31  ? -4.885  -7.104  -25.937 1.00 30.66  ? 72  HIS   A CA  1 
ATOM   226  C  C   . HIS   A 1 31  ? -4.942  -7.126  -24.417 1.00 33.93  ? 72  HIS   A C   1 
ATOM   227  O  O   . HIS   A 1 31  ? -4.413  -8.062  -23.812 1.00 33.70  ? 72  HIS   A O   1 
ATOM   228  C  CB  . HIS   A 1 31  ? -3.467  -6.705  -26.381 1.00 31.40  ? 72  HIS   A CB  1 
ATOM   229  C  CG  . HIS   A 1 31  ? -2.919  -5.493  -25.687 1.00 36.48  ? 72  HIS   A CG  1 
ATOM   230  N  ND1 . HIS   A 1 31  ? -2.577  -5.489  -24.353 1.00 39.04  ? 72  HIS   A ND1 1 
ATOM   231  C  CD2 . HIS   A 1 31  ? -2.652  -4.245  -26.143 1.00 35.18  ? 72  HIS   A CD2 1 
ATOM   232  C  CE1 . HIS   A 1 31  ? -2.127  -4.294  -24.015 1.00 36.63  ? 72  HIS   A CE1 1 
ATOM   233  N  NE2 . HIS   A 1 31  ? -2.161  -3.520  -25.083 1.00 34.56  ? 72  HIS   A NE2 1 
ATOM   234  N  N   . ALA   A 1 32  ? -5.549  -6.121  -23.785 1.00 31.25  ? 73  ALA   A N   1 
ATOM   235  C  CA  . ALA   A 1 32  ? -5.600  -6.050  -22.331 1.00 32.94  ? 73  ALA   A CA  1 
ATOM   236  C  C   . ALA   A 1 32  ? -6.957  -6.416  -21.750 1.00 28.42  ? 73  ALA   A C   1 
ATOM   237  O  O   . ALA   A 1 32  ? -7.058  -6.603  -20.534 1.00 33.10  ? 73  ALA   A O   1 
ATOM   238  C  CB  . ALA   A 1 32  ? -5.211  -4.646  -21.846 1.00 35.40  ? 73  ALA   A CB  1 
ATOM   239  N  N   . CYS   A 1 33  ? -7.996  -6.517  -22.574 1.00 31.80  ? 74  CYS   A N   1 
ATOM   240  C  CA  . CYS   A 1 33  ? -9.335  -6.835  -22.104 1.00 29.62  ? 74  CYS   A CA  1 
ATOM   241  C  C   . CYS   A 1 33  ? -9.872  -8.025  -22.884 1.00 32.88  ? 74  CYS   A C   1 
ATOM   242  O  O   . CYS   A 1 33  ? -9.362  -8.382  -23.947 1.00 31.84  ? 74  CYS   A O   1 
ATOM   243  C  CB  . CYS   A 1 33  ? -10.283 -5.636  -22.252 1.00 35.71  ? 74  CYS   A CB  1 
ATOM   244  S  SG  . CYS   A 1 33  ? -9.718  -4.123  -21.434 1.00 30.67  ? 74  CYS   A SG  1 
ATOM   245  N  N   . VAL   A 1 34  ? -10.918 -8.637  -22.341 1.00 29.26  ? 75  VAL   A N   1 
ATOM   246  C  CA  . VAL   A 1 34  ? -11.588 -9.755  -22.998 1.00 34.13  ? 75  VAL   A CA  1 
ATOM   247  C  C   . VAL   A 1 34  ? -12.802 -9.188  -23.727 1.00 34.00  ? 75  VAL   A C   1 
ATOM   248  O  O   . VAL   A 1 34  ? -13.150 -8.020  -23.506 1.00 35.59  ? 75  VAL   A O   1 
ATOM   249  C  CB  . VAL   A 1 34  ? -11.981 -10.844 -21.985 1.00 33.99  ? 75  VAL   A CB  1 
ATOM   250  C  CG1 . VAL   A 1 34  ? -10.731 -11.483 -21.388 1.00 34.67  ? 75  VAL   A CG1 1 
ATOM   251  C  CG2 . VAL   A 1 34  ? -12.876 -10.276 -20.895 1.00 34.76  ? 75  VAL   A CG2 1 
ATOM   252  N  N   . PRO   A 1 35  ? -13.460 -9.940  -24.611 1.00 41.60  ? 76  PRO   A N   1 
ATOM   253  C  CA  . PRO   A 1 35  ? -14.740 -9.471  -25.155 1.00 39.28  ? 76  PRO   A CA  1 
ATOM   254  C  C   . PRO   A 1 35  ? -15.751 -9.216  -24.044 1.00 37.47  ? 76  PRO   A C   1 
ATOM   255  O  O   . PRO   A 1 35  ? -15.700 -9.836  -22.980 1.00 38.91  ? 76  PRO   A O   1 
ATOM   256  C  CB  . PRO   A 1 35  ? -15.173 -10.629 -26.061 1.00 41.72  ? 76  PRO   A CB  1 
ATOM   257  C  CG  . PRO   A 1 35  ? -13.870 -11.179 -26.520 1.00 38.05  ? 76  PRO   A CG  1 
ATOM   258  C  CD  . PRO   A 1 35  ? -13.040 -11.191 -25.272 1.00 38.91  ? 76  PRO   A CD  1 
ATOM   259  N  N   . THR   A 1 36  ? -16.660 -8.272  -24.288 1.00 40.83  ? 77  THR   A N   1 
ATOM   260  C  CA  . THR   A 1 36  ? -17.715 -8.010  -23.320 1.00 44.91  ? 77  THR   A CA  1 
ATOM   261  C  C   . THR   A 1 36  ? -18.621 -9.226  -23.186 1.00 46.85  ? 77  THR   A C   1 
ATOM   262  O  O   . THR   A 1 36  ? -18.817 -9.986  -24.137 1.00 41.86  ? 77  THR   A O   1 
ATOM   263  C  CB  . THR   A 1 36  ? -18.544 -6.791  -23.721 1.00 48.01  ? 77  THR   A CB  1 
ATOM   264  O  OG1 . THR   A 1 36  ? -18.981 -6.925  -25.080 1.00 51.89  ? 77  THR   A OG1 1 
ATOM   265  C  CG2 . THR   A 1 36  ? -17.754 -5.512  -23.550 1.00 43.51  ? 77  THR   A CG2 1 
ATOM   266  N  N   . ASP   A 1 37  ? -19.141 -9.423  -21.978 1.00 51.48  ? 78  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 37  ? -20.114 -10.478 -21.741 1.00 50.36  ? 78  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 37  ? -21.255 -10.309 -22.738 1.00 50.26  ? 78  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 37  ? -21.913 -9.257  -22.743 1.00 47.68  ? 78  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 37  ? -20.638 -10.428 -20.305 1.00 52.02  ? 78  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 37  ? -21.523 -11.613 -19.960 1.00 56.41  ? 78  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 37  ? -21.856 -12.408 -20.864 1.00 54.67  ? 78  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 37  ? -21.892 -11.751 -18.773 1.00 55.03  ? 78  ASP   A OD2 1 
ATOM   274  N  N   . PRO   A 1 38  ? -21.495 -11.284 -23.622 1.00 51.00  ? 79  PRO   A N   1 
ATOM   275  C  CA  . PRO   A 1 38  ? -22.641 -11.179 -24.536 1.00 52.63  ? 79  PRO   A CA  1 
ATOM   276  C  C   . PRO   A 1 38  ? -23.975 -11.434 -23.861 1.00 54.11  ? 79  PRO   A C   1 
ATOM   277  O  O   . PRO   A 1 38  ? -25.011 -11.002 -24.384 1.00 59.78  ? 79  PRO   A O   1 
ATOM   278  C  CB  . PRO   A 1 38  ? -22.345 -12.253 -25.592 1.00 53.20  ? 79  PRO   A CB  1 
ATOM   279  C  CG  . PRO   A 1 38  ? -21.530 -13.272 -24.864 1.00 54.92  ? 79  PRO   A CG  1 
ATOM   280  C  CD  . PRO   A 1 38  ? -20.764 -12.552 -23.785 1.00 54.10  ? 79  PRO   A CD  1 
ATOM   281  N  N   . ASN   A 1 39  ? -23.975 -12.108 -22.714 1.00 49.74  ? 80  ASN   A N   1 
ATOM   282  C  CA  . ASN   A 1 39  ? -25.184 -12.437 -21.958 1.00 55.18  ? 80  ASN   A CA  1 
ATOM   283  C  C   . ASN   A 1 39  ? -25.071 -11.935 -20.525 1.00 55.01  ? 80  ASN   A C   1 
ATOM   284  O  O   . ASN   A 1 39  ? -25.024 -12.732 -19.580 1.00 56.16  ? 80  ASN   A O   1 
ATOM   285  C  CB  . ASN   A 1 39  ? -25.432 -13.946 -21.986 1.00 61.06  ? 80  ASN   A CB  1 
ATOM   286  C  CG  . ASN   A 1 39  ? -26.832 -14.319 -21.554 1.00 68.97  ? 80  ASN   A CG  1 
ATOM   287  O  OD1 . ASN   A 1 39  ? -27.812 -13.762 -22.020 1.00 70.00  ? 80  ASN   A OD1 1 
ATOM   288  N  ND2 . ASN   A 1 39  ? -26.925 -15.304 -20.674 1.00 66.58  ? 80  ASN   A ND2 1 
ATOM   289  N  N   . PRO   A 1 40  ? -25.044 -10.617 -20.323 1.00 56.79  ? 81  PRO   A N   1 
ATOM   290  C  CA  . PRO   A 1 40  ? -24.985 -10.093 -18.959 1.00 53.70  ? 81  PRO   A CA  1 
ATOM   291  C  C   . PRO   A 1 40  ? -26.369 -10.059 -18.333 1.00 50.65  ? 81  PRO   A C   1 
ATOM   292  O  O   . PRO   A 1 40  ? -27.371 -9.786  -18.996 1.00 52.31  ? 81  PRO   A O   1 
ATOM   293  C  CB  . PRO   A 1 40  ? -24.420 -8.680  -19.149 1.00 52.22  ? 81  PRO   A CB  1 
ATOM   294  C  CG  . PRO   A 1 40  ? -24.917 -8.275  -20.488 1.00 52.39  ? 81  PRO   A CG  1 
ATOM   295  C  CD  . PRO   A 1 40  ? -25.064 -9.535  -21.320 1.00 52.13  ? 81  PRO   A CD  1 
ATOM   296  N  N   . GLN   A 1 41  ? -26.421 -10.353 -17.039 1.00 53.64  ? 82  GLN   A N   1 
ATOM   297  C  CA  . GLN   A 1 41  ? -27.688 -10.310 -16.317 1.00 53.75  ? 82  GLN   A CA  1 
ATOM   298  C  C   . GLN   A 1 41  ? -27.379 -9.999  -14.861 1.00 51.96  ? 82  GLN   A C   1 
ATOM   299  O  O   . GLN   A 1 41  ? -26.766 -10.817 -14.172 1.00 57.61  ? 82  GLN   A O   1 
ATOM   300  C  CB  . GLN   A 1 41  ? -28.446 -11.628 -16.445 1.00 51.57  ? 82  GLN   A CB  1 
ATOM   301  C  CG  . GLN   A 1 41  ? -29.691 -11.692 -15.581 1.00 49.05  ? 82  GLN   A CG  1 
ATOM   302  C  CD  . GLN   A 1 41  ? -30.530 -10.434 -15.696 1.00 57.00  ? 82  GLN   A CD  1 
ATOM   303  O  OE1 . GLN   A 1 41  ? -30.856 -9.993  -16.801 1.00 58.09  ? 82  GLN   A OE1 1 
ATOM   304  N  NE2 . GLN   A 1 41  ? -30.876 -9.845  -14.560 1.00 54.23  ? 82  GLN   A NE2 1 
ATOM   305  N  N   . GLU   A 1 42  ? -27.794 -8.824  -14.400 1.00 51.24  ? 83  GLU   A N   1 
ATOM   306  C  CA  . GLU   A 1 42  ? -27.626 -8.480  -12.999 1.00 49.37  ? 83  GLU   A CA  1 
ATOM   307  C  C   . GLU   A 1 42  ? -28.600 -9.282  -12.137 1.00 53.11  ? 83  GLU   A C   1 
ATOM   308  O  O   . GLU   A 1 42  ? -29.592 -9.828  -12.623 1.00 54.29  ? 83  GLU   A O   1 
ATOM   309  C  CB  . GLU   A 1 42  ? -27.809 -6.972  -12.799 1.00 52.07  ? 83  GLU   A CB  1 
ATOM   310  C  CG  . GLU   A 1 42  ? -29.235 -6.482  -12.616 1.00 52.93  ? 83  GLU   A CG  1 
ATOM   311  C  CD  . GLU   A 1 42  ? -29.337 -4.971  -12.767 1.00 57.01  ? 83  GLU   A CD  1 
ATOM   312  O  OE1 . GLU   A 1 42  ? -29.248 -4.478  -13.912 1.00 54.16  ? 83  GLU   A OE1 1 
ATOM   313  O  OE2 . GLU   A 1 42  ? -29.493 -4.275  -11.742 1.00 56.31  ? 83  GLU   A OE2 1 
ATOM   314  N  N   . ILE   A 1 43  ? -28.299 -9.369  -10.844 1.00 51.80  ? 84  ILE   A N   1 
ATOM   315  C  CA  . ILE   A 1 43  ? -29.114 -10.130 -9.902  1.00 52.78  ? 84  ILE   A CA  1 
ATOM   316  C  C   . ILE   A 1 43  ? -29.555 -9.184  -8.796  1.00 53.21  ? 84  ILE   A C   1 
ATOM   317  O  O   . ILE   A 1 43  ? -28.729 -8.747  -7.985  1.00 53.70  ? 84  ILE   A O   1 
ATOM   318  C  CB  . ILE   A 1 43  ? -28.364 -11.339 -9.324  1.00 51.40  ? 84  ILE   A CB  1 
ATOM   319  C  CG1 . ILE   A 1 43  ? -28.087 -12.360 -10.425 1.00 46.89  ? 84  ILE   A CG1 1 
ATOM   320  C  CG2 . ILE   A 1 43  ? -29.166 -11.976 -8.203  1.00 50.62  ? 84  ILE   A CG2 1 
ATOM   321  C  CD1 . ILE   A 1 43  ? -27.056 -13.413 -10.051 1.00 49.73  ? 84  ILE   A CD1 1 
ATOM   322  N  N   . HIS   A 1 44  ? -30.849 -8.857  -8.763  1.00 53.64  ? 85  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 44  ? -31.352 -8.007  -7.694  1.00 49.25  ? 85  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 44  ? -31.151 -8.676  -6.343  1.00 52.56  ? 85  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 44  ? -31.366 -9.879  -6.183  1.00 52.31  ? 85  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 44  ? -32.834 -7.676  -7.877  1.00 49.90  ? 85  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 44  ? -33.379 -6.793  -6.794  1.00 54.42  ? 85  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 44  ? -32.754 -5.630  -6.400  1.00 55.10  ? 85  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 44  ? -34.475 -6.912  -6.008  1.00 57.04  ? 85  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 44  ? -33.445 -5.065  -5.426  1.00 54.34  ? 85  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 44  ? -34.496 -5.822  -5.170  1.00 59.84  ? 85  HIS   A NE2 1 
ATOM   332  N  N   . LEU   A 1 45  ? -30.730 -7.884  -5.366  1.00 52.59  ? 86  LEU   A N   1 
ATOM   333  C  CA  . LEU   A 1 45  ? -30.528 -8.365  -4.005  1.00 54.26  ? 86  LEU   A CA  1 
ATOM   334  C  C   . LEU   A 1 45  ? -31.749 -7.940  -3.194  1.00 54.33  ? 86  LEU   A C   1 
ATOM   335  O  O   . LEU   A 1 45  ? -31.744 -6.921  -2.499  1.00 50.79  ? 86  LEU   A O   1 
ATOM   336  C  CB  . LEU   A 1 45  ? -29.233 -7.797  -3.442  1.00 48.67  ? 86  LEU   A CB  1 
ATOM   337  C  CG  . LEU   A 1 45  ? -27.922 -8.026  -4.192  1.00 50.11  ? 86  LEU   A CG  1 
ATOM   338  C  CD1 . LEU   A 1 45  ? -26.740 -7.658  -3.312  1.00 50.96  ? 86  LEU   A CD1 1 
ATOM   339  C  CD2 . LEU   A 1 45  ? -27.804 -9.471  -4.665  1.00 50.68  ? 86  LEU   A CD2 1 
ATOM   340  N  N   . GLU   A 1 46  ? -32.822 -8.728  -3.323  1.00 60.00  ? 87  GLU   A N   1 
ATOM   341  C  CA  . GLU   A 1 46  ? -34.109 -8.396  -2.717  1.00 54.70  ? 87  GLU   A CA  1 
ATOM   342  C  C   . GLU   A 1 46  ? -33.948 -8.039  -1.249  1.00 57.06  ? 87  GLU   A C   1 
ATOM   343  O  O   . GLU   A 1 46  ? -33.452 -8.839  -0.451  1.00 57.59  ? 87  GLU   A O   1 
ATOM   344  C  CB  . GLU   A 1 46  ? -35.101 -9.553  -2.885  1.00 62.72  ? 87  GLU   A CB  1 
ATOM   345  C  CG  . GLU   A 1 46  ? -36.487 -9.268  -2.302  1.00 62.86  ? 87  GLU   A CG  1 
ATOM   346  C  CD  . GLU   A 1 46  ? -37.337 -8.359  -3.167  1.00 66.25  ? 87  GLU   A CD  1 
ATOM   347  O  OE1 . GLU   A 1 46  ? -37.256 -8.447  -4.412  1.00 66.08  ? 87  GLU   A OE1 1 
ATOM   348  O  OE2 . GLU   A 1 46  ? -38.101 -7.556  -2.591  1.00 64.86  ? 87  GLU   A OE2 1 
ATOM   349  N  N   . ASN   A 1 47  ? -34.336 -6.803  -0.922  1.00 58.25  ? 88  ASN   A N   1 
ATOM   350  C  CA  . ASN   A 1 47  ? -34.289 -6.249  0.436   1.00 58.56  ? 88  ASN   A CA  1 
ATOM   351  C  C   . ASN   A 1 47  ? -32.876 -6.161  1.006   1.00 58.35  ? 88  ASN   A C   1 
ATOM   352  O  O   . ASN   A 1 47  ? -32.684 -6.256  2.221   1.00 56.86  ? 88  ASN   A O   1 
ATOM   353  C  CB  . ASN   A 1 47  ? -35.166 -7.042  1.402   1.00 64.85  ? 88  ASN   A CB  1 
ATOM   354  C  CG  . ASN   A 1 47  ? -35.611 -6.210  2.592   1.00 68.49  ? 88  ASN   A CG  1 
ATOM   355  O  OD1 . ASN   A 1 47  ? -36.378 -5.259  2.453   1.00 71.79  ? 88  ASN   A OD1 1 
ATOM   356  N  ND2 . ASN   A 1 47  ? -35.085 -6.540  3.770   1.00 70.07  ? 88  ASN   A ND2 1 
ATOM   357  N  N   . VAL   A 1 48  ? -31.869 -5.974  0.164   1.00 56.53  ? 89  VAL   A N   1 
ATOM   358  C  CA  . VAL   A 1 48  ? -30.496 -5.842  0.636   1.00 53.12  ? 89  VAL   A CA  1 
ATOM   359  C  C   . VAL   A 1 48  ? -30.120 -4.371  0.654   1.00 53.44  ? 89  VAL   A C   1 
ATOM   360  O  O   . VAL   A 1 48  ? -30.203 -3.684  -0.370  1.00 49.01  ? 89  VAL   A O   1 
ATOM   361  C  CB  . VAL   A 1 48  ? -29.516 -6.659  -0.216  1.00 53.82  ? 89  VAL   A CB  1 
ATOM   362  C  CG1 . VAL   A 1 48  ? -28.091 -6.338  0.181   1.00 49.50  ? 89  VAL   A CG1 1 
ATOM   363  C  CG2 . VAL   A 1 48  ? -29.775 -8.137  -0.006  1.00 52.57  ? 89  VAL   A CG2 1 
ATOM   364  N  N   . THR   A 1 49  ? -29.720 -3.889  1.825   1.00 51.62  ? 90  THR   A N   1 
ATOM   365  C  CA  . THR   A 1 49  ? -29.167 -2.553  1.986   1.00 50.64  ? 90  THR   A CA  1 
ATOM   366  C  C   . THR   A 1 49  ? -27.667 -2.687  2.202   1.00 50.07  ? 90  THR   A C   1 
ATOM   367  O  O   . THR   A 1 49  ? -27.226 -3.395  3.114   1.00 39.56  ? 90  THR   A O   1 
ATOM   368  C  CB  . THR   A 1 49  ? -29.825 -1.822  3.153   1.00 51.43  ? 90  THR   A CB  1 
ATOM   369  O  OG1 . THR   A 1 49  ? -31.190 -1.540  2.820   1.00 52.52  ? 90  THR   A OG1 1 
ATOM   370  C  CG2 . THR   A 1 49  ? -29.110 -0.513  3.429   1.00 50.03  ? 90  THR   A CG2 1 
ATOM   371  N  N   . GLU   A 1 50  ? -26.887 -2.022  1.355   1.00 47.23  ? 91  GLU   A N   1 
ATOM   372  C  CA  . GLU   A 1 50  ? -25.435 -2.125  1.389   1.00 46.25  ? 91  GLU   A CA  1 
ATOM   373  C  C   . GLU   A 1 50  ? -24.807 -0.742  1.352   1.00 45.90  ? 91  GLU   A C   1 
ATOM   374  O  O   . GLU   A 1 50  ? -25.270 0.142   0.628   1.00 42.13  ? 91  GLU   A O   1 
ATOM   375  C  CB  . GLU   A 1 50  ? -24.913 -2.973  0.225   1.00 48.22  ? 91  GLU   A CB  1 
ATOM   376  C  CG  . GLU   A 1 50  ? -23.418 -3.267  0.286   1.00 51.92  ? 91  GLU   A CG  1 
ATOM   377  C  CD  . GLU   A 1 50  ? -23.091 -4.377  1.256   1.00 51.44  ? 91  GLU   A CD  1 
ATOM   378  O  OE1 . GLU   A 1 50  ? -23.993 -5.187  1.532   1.00 52.85  ? 91  GLU   A OE1 1 
ATOM   379  O  OE2 . GLU   A 1 50  ? -21.929 -4.470  1.715   1.00 55.53  ? 91  GLU   A OE2 1 
ATOM   380  N  N   . ASN   A 1 51  ? -23.743 -0.571  2.134   1.00 38.53  ? 92  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? -23.016 0.687   2.192   1.00 41.93  ? 92  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? -21.998 0.750   1.063   1.00 41.28  ? 92  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? -21.342 -0.245  0.747   1.00 40.69  ? 92  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? -22.289 0.854   3.527   1.00 45.64  ? 92  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? -23.206 1.271   4.643   1.00 50.28  ? 92  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? -22.866 1.149   5.815   1.00 57.94  ? 92  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? -24.387 1.724   4.294   1.00 47.89  ? 92  ASN   A ND2 1 
ATOM   388  N  N   . PHE   A 1 52  ? -21.861 1.930   0.470   1.00 45.82  ? 93  PHE   A N   1 
ATOM   389  C  CA  . PHE   A 1 52  ? -20.908 2.163   -0.600  1.00 40.83  ? 93  PHE   A CA  1 
ATOM   390  C  C   . PHE   A 1 52  ? -20.039 3.353   -0.214  1.00 43.02  ? 93  PHE   A C   1 
ATOM   391  O  O   . PHE   A 1 52  ? -20.434 4.195   0.594   1.00 38.96  ? 93  PHE   A O   1 
ATOM   392  C  CB  . PHE   A 1 52  ? -21.619 2.443   -1.928  1.00 42.22  ? 93  PHE   A CB  1 
ATOM   393  C  CG  . PHE   A 1 52  ? -22.214 1.226   -2.573  1.00 42.82  ? 93  PHE   A CG  1 
ATOM   394  C  CD1 . PHE   A 1 52  ? -23.385 0.675   -2.078  1.00 42.14  ? 93  PHE   A CD1 1 
ATOM   395  C  CD2 . PHE   A 1 52  ? -21.626 0.648   -3.680  1.00 38.24  ? 93  PHE   A CD2 1 
ATOM   396  C  CE1 . PHE   A 1 52  ? -23.949 -0.440  -2.668  1.00 42.23  ? 93  PHE   A CE1 1 
ATOM   397  C  CE2 . PHE   A 1 52  ? -22.187 -0.468  -4.274  1.00 41.18  ? 93  PHE   A CE2 1 
ATOM   398  C  CZ  . PHE   A 1 52  ? -23.349 -1.012  -3.768  1.00 41.44  ? 93  PHE   A CZ  1 
ATOM   399  N  N   . ASN   A 1 53  ? -18.844 3.426   -0.801  1.00 39.55  ? 94  ASN   A N   1 
ATOM   400  C  CA  . ASN   A 1 53  ? -17.987 4.597   -0.610  1.00 36.35  ? 94  ASN   A CA  1 
ATOM   401  C  C   . ASN   A 1 53  ? -17.210 4.803   -1.908  1.00 36.67  ? 94  ASN   A C   1 
ATOM   402  O  O   . ASN   A 1 53  ? -16.214 4.116   -2.152  1.00 39.95  ? 94  ASN   A O   1 
ATOM   403  C  CB  . ASN   A 1 53  ? -17.062 4.424   0.588   1.00 30.77  ? 94  ASN   A CB  1 
ATOM   404  C  CG  . ASN   A 1 53  ? -16.264 5.679   0.896   1.00 38.53  ? 94  ASN   A CG  1 
ATOM   405  O  OD1 . ASN   A 1 53  ? -16.314 6.664   0.155   1.00 38.19  ? 94  ASN   A OD1 1 
ATOM   406  N  ND2 . ASN   A 1 53  ? -15.523 5.650   1.999   1.00 41.48  ? 94  ASN   A ND2 1 
ATOM   407  N  N   . MET   A 1 54  ? -17.679 5.748   -2.730  1.00 37.51  ? 95  MET   A N   1 
ATOM   408  C  CA  . MET   A 1 54  ? -17.023 6.045   -3.998  1.00 36.47  ? 95  MET   A CA  1 
ATOM   409  C  C   . MET   A 1 54  ? -15.679 6.720   -3.787  1.00 35.14  ? 95  MET   A C   1 
ATOM   410  O  O   . MET   A 1 54  ? -14.815 6.654   -4.666  1.00 38.19  ? 95  MET   A O   1 
ATOM   411  C  CB  . MET   A 1 54  ? -17.920 6.939   -4.853  1.00 34.69  ? 95  MET   A CB  1 
ATOM   412  C  CG  . MET   A 1 54  ? -18.447 8.146   -4.111  1.00 34.79  ? 95  MET   A CG  1 
ATOM   413  S  SD  . MET   A 1 54  ? -19.015 9.551   -5.102  1.00 35.22  ? 95  MET   A SD  1 
ATOM   414  C  CE  . MET   A 1 54  ? -17.779 9.682   -6.373  1.00 38.20  ? 95  MET   A CE  1 
ATOM   415  N  N   . TRP   A 1 55  ? -15.485 7.355   -2.635  1.00 36.33  ? 96  TRP   A N   1 
ATOM   416  C  CA  . TRP   A 1 55  ? -14.255 8.067   -2.321  1.00 36.07  ? 96  TRP   A CA  1 
ATOM   417  C  C   . TRP   A 1 55  ? -13.192 7.153   -1.734  1.00 39.32  ? 96  TRP   A C   1 
ATOM   418  O  O   . TRP   A 1 55  ? -12.040 7.575   -1.589  1.00 39.97  ? 96  TRP   A O   1 
ATOM   419  C  CB  . TRP   A 1 55  ? -14.571 9.219   -1.361  1.00 40.02  ? 96  TRP   A CB  1 
ATOM   420  C  CG  . TRP   A 1 55  ? -15.524 10.177  -1.992  1.00 41.29  ? 96  TRP   A CG  1 
ATOM   421  C  CD1 . TRP   A 1 55  ? -16.874 10.234  -1.798  1.00 40.94  ? 96  TRP   A CD1 1 
ATOM   422  C  CD2 . TRP   A 1 55  ? -15.213 11.187  -2.953  1.00 36.34  ? 96  TRP   A CD2 1 
ATOM   423  N  NE1 . TRP   A 1 55  ? -17.421 11.227  -2.575  1.00 33.57  ? 96  TRP   A NE1 1 
ATOM   424  C  CE2 . TRP   A 1 55  ? -16.420 11.827  -3.292  1.00 36.46  ? 96  TRP   A CE2 1 
ATOM   425  C  CE3 . TRP   A 1 55  ? -14.028 11.623  -3.551  1.00 39.16  ? 96  TRP   A CE3 1 
ATOM   426  C  CZ2 . TRP   A 1 55  ? -16.476 12.869  -4.211  1.00 36.07  ? 96  TRP   A CZ2 1 
ATOM   427  C  CZ3 . TRP   A 1 55  ? -14.087 12.657  -4.459  1.00 37.36  ? 96  TRP   A CZ3 1 
ATOM   428  C  CH2 . TRP   A 1 55  ? -15.302 13.272  -4.776  1.00 38.96  ? 96  TRP   A CH2 1 
ATOM   429  N  N   . LYS   A 1 56  ? -13.553 5.907   -1.418  1.00 42.11  ? 97  LYS   A N   1 
ATOM   430  C  CA  . LYS   A 1 56  ? -12.632 4.887   -0.923  1.00 42.92  ? 97  LYS   A CA  1 
ATOM   431  C  C   . LYS   A 1 56  ? -13.050 3.577   -1.595  1.00 39.16  ? 97  LYS   A C   1 
ATOM   432  O  O   . LYS   A 1 56  ? -13.736 2.734   -1.012  1.00 38.00  ? 97  LYS   A O   1 
ATOM   433  C  CB  . LYS   A 1 56  ? -12.671 4.790   0.598   1.00 49.74  ? 97  LYS   A CB  1 
ATOM   434  C  CG  . LYS   A 1 56  ? -11.890 5.881   1.302   1.00 48.66  ? 97  LYS   A CG  1 
ATOM   435  C  CD  . LYS   A 1 56  ? -11.586 5.498   2.744   1.00 61.26  ? 97  LYS   A CD  1 
ATOM   436  C  CE  . LYS   A 1 56  ? -10.344 6.200   3.255   1.00 73.40  ? 97  LYS   A CE  1 
ATOM   437  N  NZ  . LYS   A 1 56  ? -10.699 7.337   4.140   1.00 69.84  ? 97  LYS   A NZ  1 
ATOM   438  N  N   . ASN   A 1 57  ? -12.629 3.409   -2.846  1.00 41.80  ? 98  ASN   A N   1 
ATOM   439  C  CA  . ASN   A 1 57  ? -13.085 2.306   -3.682  1.00 33.90  ? 98  ASN   A CA  1 
ATOM   440  C  C   . ASN   A 1 57  ? -11.887 1.828   -4.484  1.00 38.01  ? 98  ASN   A C   1 
ATOM   441  O  O   . ASN   A 1 57  ? -11.336 2.599   -5.274  1.00 36.48  ? 98  ASN   A O   1 
ATOM   442  C  CB  . ASN   A 1 57  ? -14.209 2.763   -4.617  1.00 35.22  ? 98  ASN   A CB  1 
ATOM   443  C  CG  . ASN   A 1 57  ? -14.815 1.627   -5.409  1.00 35.95  ? 98  ASN   A CG  1 
ATOM   444  O  OD1 . ASN   A 1 57  ? -14.210 0.567   -5.554  1.00 36.11  ? 98  ASN   A OD1 1 
ATOM   445  N  ND2 . ASN   A 1 57  ? -15.999 1.858   -5.964  1.00 37.21  ? 98  ASN   A ND2 1 
ATOM   446  N  N   . ASN   A 1 58  ? -11.487 0.566   -4.287  1.00 35.50  ? 99  ASN   A N   1 
ATOM   447  C  CA  . ASN   A 1 58  ? -10.300 0.062   -4.976  1.00 37.18  ? 99  ASN   A CA  1 
ATOM   448  C  C   . ASN   A 1 58  ? -10.493 0.012   -6.488  1.00 34.66  ? 99  ASN   A C   1 
ATOM   449  O  O   . ASN   A 1 58  ? -9.510  0.090   -7.238  1.00 34.65  ? 99  ASN   A O   1 
ATOM   450  C  CB  . ASN   A 1 58  ? -9.917  -1.321  -4.458  1.00 35.38  ? 99  ASN   A CB  1 
ATOM   451  C  CG  . ASN   A 1 58  ? -8.577  -1.783  -4.995  1.00 35.33  ? 99  ASN   A CG  1 
ATOM   452  O  OD1 . ASN   A 1 58  ? -8.501  -2.746  -5.758  1.00 39.99  ? 99  ASN   A OD1 1 
ATOM   453  N  ND2 . ASN   A 1 58  ? -7.512  -1.083  -4.613  1.00 36.51  ? 99  ASN   A ND2 1 
ATOM   454  N  N   . MET   A 1 59  ? -11.742 -0.121  -6.951  1.00 29.89  ? 100 MET   A N   1 
ATOM   455  C  CA  . MET   A 1 59  ? -12.018 -0.116  -8.385  1.00 32.62  ? 100 MET   A CA  1 
ATOM   456  C  C   . MET   A 1 59  ? -11.439 1.124   -9.052  1.00 32.76  ? 100 MET   A C   1 
ATOM   457  O  O   . MET   A 1 59  ? -10.822 1.040   -10.121 1.00 31.25  ? 100 MET   A O   1 
ATOM   458  C  CB  . MET   A 1 59  ? -13.524 -0.207  -8.626  1.00 33.22  ? 100 MET   A CB  1 
ATOM   459  C  CG  . MET   A 1 59  ? -14.222 -1.258  -7.793  1.00 35.27  ? 100 MET   A CG  1 
ATOM   460  S  SD  . MET   A 1 59  ? -15.956 -1.453  -8.226  1.00 38.54  ? 100 MET   A SD  1 
ATOM   461  C  CE  . MET   A 1 59  ? -15.847 -1.920  -9.947  1.00 27.79  ? 100 MET   A CE  1 
ATOM   462  N  N   . VAL   A 1 60  ? -11.605 2.283   -8.407  1.00 32.21  ? 101 VAL   A N   1 
ATOM   463  C  CA  . VAL   A 1 60  ? -11.107 3.543   -8.955  1.00 31.78  ? 101 VAL   A CA  1 
ATOM   464  C  C   . VAL   A 1 60  ? -9.603  3.470   -9.184  1.00 34.71  ? 101 VAL   A C   1 
ATOM   465  O  O   . VAL   A 1 60  ? -9.095  3.866   -10.241 1.00 30.90  ? 101 VAL   A O   1 
ATOM   466  C  CB  . VAL   A 1 60  ? -11.477 4.711   -8.024  1.00 34.02  ? 101 VAL   A CB  1 
ATOM   467  C  CG1 . VAL   A 1 60  ? -10.842 6.005   -8.515  1.00 33.19  ? 101 VAL   A CG1 1 
ATOM   468  C  CG2 . VAL   A 1 60  ? -12.980 4.854   -7.938  1.00 31.54  ? 101 VAL   A CG2 1 
ATOM   469  N  N   . GLU   A 1 61  ? -8.867  2.958   -8.192  1.00 38.05  ? 102 GLU   A N   1 
ATOM   470  C  CA  . GLU   A 1 61  ? -7.421  2.837   -8.340  1.00 35.39  ? 102 GLU   A CA  1 
ATOM   471  C  C   . GLU   A 1 61  ? -7.071  1.847   -9.444  1.00 33.00  ? 102 GLU   A C   1 
ATOM   472  O  O   . GLU   A 1 61  ? -6.113  2.058   -10.199 1.00 33.07  ? 102 GLU   A O   1 
ATOM   473  C  CB  . GLU   A 1 61  ? -6.796  2.419   -7.011  1.00 38.59  ? 102 GLU   A CB  1 
ATOM   474  C  CG  . GLU   A 1 61  ? -6.251  3.590   -6.210  1.00 45.54  ? 102 GLU   A CG  1 
ATOM   475  C  CD  . GLU   A 1 61  ? -7.349  4.357   -5.495  1.00 47.75  ? 102 GLU   A CD  1 
ATOM   476  O  OE1 . GLU   A 1 61  ? -8.457  3.804   -5.313  1.00 49.78  ? 102 GLU   A OE1 1 
ATOM   477  O  OE2 . GLU   A 1 61  ? -7.109  5.525   -5.122  1.00 43.58  ? 102 GLU   A OE2 1 
ATOM   478  N  N   . GLN   A 1 62  ? -7.861  0.773   -9.572  1.00 33.17  ? 103 GLN   A N   1 
ATOM   479  C  CA  . GLN   A 1 62  ? -7.597  -0.229  -10.601 1.00 34.51  ? 103 GLN   A CA  1 
ATOM   480  C  C   . GLN   A 1 62  ? -7.932  0.290   -11.994 1.00 33.44  ? 103 GLN   A C   1 
ATOM   481  O  O   . GLN   A 1 62  ? -7.293  -0.099  -12.978 1.00 31.77  ? 103 GLN   A O   1 
ATOM   482  C  CB  . GLN   A 1 62  ? -8.372  -1.511  -10.315 1.00 31.46  ? 103 GLN   A CB  1 
ATOM   483  C  CG  . GLN   A 1 62  ? -7.822  -2.335  -9.173  1.00 38.62  ? 103 GLN   A CG  1 
ATOM   484  C  CD  . GLN   A 1 62  ? -8.347  -3.751  -9.201  1.00 36.44  ? 103 GLN   A CD  1 
ATOM   485  O  OE1 . GLN   A 1 62  ? -8.372  -4.398  -10.251 1.00 37.49  ? 103 GLN   A OE1 1 
ATOM   486  N  NE2 . GLN   A 1 62  ? -8.782  -4.239  -8.047  1.00 37.08  ? 103 GLN   A NE2 1 
ATOM   487  N  N   . MET   A 1 63  ? -8.943  1.146   -12.113 1.00 28.79  ? 104 MET   A N   1 
ATOM   488  C  CA  . MET   A 1 63  ? -9.158  1.790   -13.400 1.00 30.36  ? 104 MET   A CA  1 
ATOM   489  C  C   . MET   A 1 63  ? -8.063  2.809   -13.675 1.00 26.43  ? 104 MET   A C   1 
ATOM   490  O  O   . MET   A 1 63  ? -7.611  2.960   -14.818 1.00 29.90  ? 104 MET   A O   1 
ATOM   491  C  CB  . MET   A 1 63  ? -10.535 2.440   -13.443 1.00 28.17  ? 104 MET   A CB  1 
ATOM   492  C  CG  . MET   A 1 63  ? -10.756 3.244   -14.710 1.00 32.32  ? 104 MET   A CG  1 
ATOM   493  S  SD  . MET   A 1 63  ? -12.478 3.679   -14.964 1.00 32.31  ? 104 MET   A SD  1 
ATOM   494  C  CE  . MET   A 1 63  ? -12.424 4.181   -16.683 1.00 26.66  ? 104 MET   A CE  1 
ATOM   495  N  N   . HIS   A 1 64  ? -7.598  3.489   -12.626 1.00 28.21  ? 105 HIS   A N   1 
ATOM   496  C  CA  . HIS   A 1 64  ? -6.560  4.498   -12.789 1.00 28.43  ? 105 HIS   A CA  1 
ATOM   497  C  C   . HIS   A 1 64  ? -5.284  3.878   -13.347 1.00 30.48  ? 105 HIS   A C   1 
ATOM   498  O  O   . HIS   A 1 64  ? -4.680  4.417   -14.282 1.00 26.26  ? 105 HIS   A O   1 
ATOM   499  C  CB  . HIS   A 1 64  ? -6.307  5.182   -11.445 1.00 30.73  ? 105 HIS   A CB  1 
ATOM   500  C  CG  . HIS   A 1 64  ? -5.490  6.436   -11.534 1.00 31.15  ? 105 HIS   A CG  1 
ATOM   501  N  ND1 . HIS   A 1 64  ? -5.933  7.569   -12.178 1.00 28.67  ? 105 HIS   A ND1 1 
ATOM   502  C  CD2 . HIS   A 1 64  ? -4.273  6.747   -11.029 1.00 27.96  ? 105 HIS   A CD2 1 
ATOM   503  C  CE1 . HIS   A 1 64  ? -5.019  8.519   -12.081 1.00 32.13  ? 105 HIS   A CE1 1 
ATOM   504  N  NE2 . HIS   A 1 64  ? -4.000  8.045   -11.389 1.00 35.23  ? 105 HIS   A NE2 1 
ATOM   505  N  N   . GLU   A 1 65  ? -4.865  2.731   -12.790 1.00 30.63  ? 106 GLU   A N   1 
ATOM   506  C  CA  . GLU   A 1 65  ? -3.687  2.035   -13.308 1.00 31.03  ? 106 GLU   A CA  1 
ATOM   507  C  C   . GLU   A 1 65  ? -3.881  1.617   -14.765 1.00 27.45  ? 106 GLU   A C   1 
ATOM   508  O  O   . GLU   A 1 65  ? -2.935  1.668   -15.563 1.00 27.36  ? 106 GLU   A O   1 
ATOM   509  C  CB  . GLU   A 1 65  ? -3.354  0.820   -12.433 1.00 30.67  ? 106 GLU   A CB  1 
ATOM   510  C  CG  . GLU   A 1 65  ? -4.530  -0.106  -12.223 1.00 39.69  ? 106 GLU   A CG  1 
ATOM   511  C  CD  . GLU   A 1 65  ? -4.186  -1.494  -11.703 1.00 49.29  ? 106 GLU   A CD  1 
ATOM   512  O  OE1 . GLU   A 1 65  ? -3.264  -1.631  -10.869 1.00 59.57  ? 106 GLU   A OE1 1 
ATOM   513  O  OE2 . GLU   A 1 65  ? -4.876  -2.455  -12.115 1.00 43.64  ? 106 GLU   A OE2 1 
ATOM   514  N  N   . ASP   A 1 66  ? -5.104  1.217   -15.137 1.00 28.08  ? 107 ASP   A N   1 
ATOM   515  C  CA  . ASP   A 1 66  ? -5.374  0.852   -16.528 1.00 26.64  ? 107 ASP   A CA  1 
ATOM   516  C  C   . ASP   A 1 66  ? -5.180  2.036   -17.463 1.00 26.34  ? 107 ASP   A C   1 
ATOM   517  O  O   . ASP   A 1 66  ? -4.524  1.919   -18.506 1.00 23.57  ? 107 ASP   A O   1 
ATOM   518  C  CB  . ASP   A 1 66  ? -6.794  0.317   -16.682 1.00 26.96  ? 107 ASP   A CB  1 
ATOM   519  C  CG  . ASP   A 1 66  ? -6.920  -1.128  -16.280 1.00 30.79  ? 107 ASP   A CG  1 
ATOM   520  O  OD1 . ASP   A 1 66  ? -5.904  -1.747  -15.903 1.00 31.29  ? 107 ASP   A OD1 1 
ATOM   521  O  OD2 . ASP   A 1 66  ? -8.047  -1.657  -16.370 1.00 31.16  ? 107 ASP   A OD2 1 
ATOM   522  N  N   . ILE   A 1 67  ? -5.788  3.174   -17.131 1.00 27.54  ? 108 ILE   A N   1 
ATOM   523  C  CA  . ILE   A 1 67  ? -5.718  4.319   -18.030 1.00 25.29  ? 108 ILE   A CA  1 
ATOM   524  C  C   . ILE   A 1 67  ? -4.302  4.871   -18.066 1.00 28.98  ? 108 ILE   A C   1 
ATOM   525  O  O   . ILE   A 1 67  ? -3.840  5.357   -19.105 1.00 28.93  ? 108 ILE   A O   1 
ATOM   526  C  CB  . ILE   A 1 67  ? -6.746  5.392   -17.625 1.00 24.41  ? 108 ILE   A CB  1 
ATOM   527  C  CG1 . ILE   A 1 67  ? -8.099  4.752   -17.299 1.00 27.83  ? 108 ILE   A CG1 1 
ATOM   528  C  CG2 . ILE   A 1 67  ? -6.896  6.430   -18.726 1.00 23.32  ? 108 ILE   A CG2 1 
ATOM   529  C  CD1 . ILE   A 1 67  ? -8.587  3.751   -18.342 1.00 25.43  ? 108 ILE   A CD1 1 
ATOM   530  N  N   . ILE   A 1 68  ? -3.583  4.790   -16.941 1.00 32.01  ? 109 ILE   A N   1 
ATOM   531  C  CA  . ILE   A 1 68  ? -2.159  5.116   -16.958 1.00 28.86  ? 109 ILE   A CA  1 
ATOM   532  C  C   . ILE   A 1 68  ? -1.427  4.205   -17.934 1.00 31.44  ? 109 ILE   A C   1 
ATOM   533  O  O   . ILE   A 1 68  ? -0.701  4.670   -18.824 1.00 29.90  ? 109 ILE   A O   1 
ATOM   534  C  CB  . ILE   A 1 68  ? -1.558  5.049   -15.544 1.00 29.11  ? 109 ILE   A CB  1 
ATOM   535  C  CG1 . ILE   A 1 68  ? -2.153  6.146   -14.660 1.00 30.20  ? 109 ILE   A CG1 1 
ATOM   536  C  CG2 . ILE   A 1 68  ? -0.047  5.225   -15.623 1.00 33.70  ? 109 ILE   A CG2 1 
ATOM   537  C  CD1 . ILE   A 1 68  ? -1.674  6.078   -13.229 1.00 35.10  ? 109 ILE   A CD1 1 
ATOM   538  N  N   . SER   A 1 69  ? -1.639  2.892   -17.802 1.00 34.73  ? 110 SER   A N   1 
ATOM   539  C  CA  . SER   A 1 69  ? -1.045  1.940   -18.735 1.00 29.91  ? 110 SER   A CA  1 
ATOM   540  C  C   . SER   A 1 69  ? -1.496  2.213   -20.167 1.00 32.52  ? 110 SER   A C   1 
ATOM   541  O  O   . SER   A 1 69  ? -0.681  2.169   -21.098 1.00 30.67  ? 110 SER   A O   1 
ATOM   542  C  CB  . SER   A 1 69  ? -1.401  0.512   -18.317 1.00 29.00  ? 110 SER   A CB  1 
ATOM   543  O  OG  . SER   A 1 69  ? -0.969  -0.426  -19.280 1.00 40.75  ? 110 SER   A OG  1 
ATOM   544  N  N   . LEU   A 1 70  ? -2.791  2.501   -20.364 1.00 28.91  ? 111 LEU   A N   1 
ATOM   545  C  CA  . LEU   A 1 70  ? -3.305  2.757   -21.710 1.00 29.00  ? 111 LEU   A CA  1 
ATOM   546  C  C   . LEU   A 1 70  ? -2.597  3.945   -22.356 1.00 30.94  ? 111 LEU   A C   1 
ATOM   547  O  O   . LEU   A 1 70  ? -2.069  3.838   -23.470 1.00 28.24  ? 111 LEU   A O   1 
ATOM   548  C  CB  . LEU   A 1 70  ? -4.823  2.978   -21.660 1.00 25.84  ? 111 LEU   A CB  1 
ATOM   549  C  CG  . LEU   A 1 70  ? -5.648  3.061   -22.950 1.00 31.82  ? 111 LEU   A CG  1 
ATOM   550  C  CD1 . LEU   A 1 70  ? -7.083  2.729   -22.617 1.00 28.79  ? 111 LEU   A CD1 1 
ATOM   551  C  CD2 . LEU   A 1 70  ? -5.584  4.442   -23.584 1.00 29.90  ? 111 LEU   A CD2 1 
ATOM   552  N  N   . TRP   A 1 71  ? -2.568  5.091   -21.670 1.00 28.09  ? 112 TRP   A N   1 
ATOM   553  C  CA  . TRP   A 1 71  ? -1.954  6.273   -22.267 1.00 31.57  ? 112 TRP   A CA  1 
ATOM   554  C  C   . TRP   A 1 71  ? -0.458  6.078   -22.453 1.00 34.01  ? 112 TRP   A C   1 
ATOM   555  O  O   . TRP   A 1 71  ? 0.112   6.526   -23.455 1.00 33.91  ? 112 TRP   A O   1 
ATOM   556  C  CB  . TRP   A 1 71  ? -2.207  7.496   -21.403 1.00 31.24  ? 112 TRP   A CB  1 
ATOM   557  C  CG  . TRP   A 1 71  ? -3.500  8.183   -21.630 1.00 25.75  ? 112 TRP   A CG  1 
ATOM   558  C  CD1 . TRP   A 1 71  ? -4.739  7.618   -21.663 1.00 27.70  ? 112 TRP   A CD1 1 
ATOM   559  C  CD2 . TRP   A 1 71  ? -3.699  9.590   -21.744 1.00 30.18  ? 112 TRP   A CD2 1 
ATOM   560  N  NE1 . TRP   A 1 71  ? -5.695  8.583   -21.858 1.00 25.50  ? 112 TRP   A NE1 1 
ATOM   561  C  CE2 . TRP   A 1 71  ? -5.080  9.805   -21.903 1.00 26.98  ? 112 TRP   A CE2 1 
ATOM   562  C  CE3 . TRP   A 1 71  ? -2.838  10.691  -21.750 1.00 29.06  ? 112 TRP   A CE3 1 
ATOM   563  C  CZ2 . TRP   A 1 71  ? -5.619  11.073  -22.072 1.00 26.26  ? 112 TRP   A CZ2 1 
ATOM   564  C  CZ3 . TRP   A 1 71  ? -3.373  11.943  -21.915 1.00 30.17  ? 112 TRP   A CZ3 1 
ATOM   565  C  CH2 . TRP   A 1 71  ? -4.751  12.129  -22.072 1.00 26.95  ? 112 TRP   A CH2 1 
ATOM   566  N  N   . ASP   A 1 72  ? 0.198   5.421   -21.491 1.00 35.46  ? 113 ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 72  ? 1.630   5.175   -21.620 1.00 42.46  ? 113 ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 72  ? 1.938   4.326   -22.849 1.00 37.18  ? 113 ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 72  ? 2.946   4.550   -23.529 1.00 42.16  ? 113 ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 72  ? 2.173   4.521   -20.352 1.00 41.04  ? 113 ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 72  ? 2.242   5.493   -19.182 1.00 54.66  ? 113 ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 72  ? 2.829   5.123   -18.141 1.00 61.52  ? 113 ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 72  ? 1.715   6.622   -19.302 1.00 75.57  ? 113 ASP   A OD2 1 
ATOM   574  N  N   . GLN   A 1 73  ? 1.071   3.364   -23.167 1.00 35.85  ? 114 GLN   A N   1 
ATOM   575  C  CA  . GLN   A 1 73  ? 1.282   2.550   -24.356 1.00 39.26  ? 114 GLN   A CA  1 
ATOM   576  C  C   . GLN   A 1 73  ? 0.867   3.254   -25.639 1.00 39.51  ? 114 GLN   A C   1 
ATOM   577  O  O   . GLN   A 1 73  ? 1.252   2.810   -26.726 1.00 38.07  ? 114 GLN   A O   1 
ATOM   578  C  CB  . GLN   A 1 73  ? 0.510   1.236   -24.264 1.00 37.98  ? 114 GLN   A CB  1 
ATOM   579  C  CG  . GLN   A 1 73  ? 0.916   0.305   -23.153 1.00 43.03  ? 114 GLN   A CG  1 
ATOM   580  C  CD  . GLN   A 1 73  ? -0.075  -0.828  -22.994 1.00 41.82  ? 114 GLN   A CD  1 
ATOM   581  O  OE1 . GLN   A 1 73  ? -0.659  -1.296  -23.977 1.00 42.25  ? 114 GLN   A OE1 1 
ATOM   582  N  NE2 . GLN   A 1 73  ? -0.268  -1.283  -21.760 1.00 42.84  ? 114 GLN   A NE2 1 
ATOM   583  N  N   . SER   A 1 74  ? 0.088   4.323   -25.540 1.00 34.39  ? 115 SER   A N   1 
ATOM   584  C  CA  . SER   A 1 74  ? -0.620  4.893   -26.677 1.00 35.83  ? 115 SER   A CA  1 
ATOM   585  C  C   . SER   A 1 74  ? -0.243  6.337   -26.953 1.00 37.45  ? 115 SER   A C   1 
ATOM   586  O  O   . SER   A 1 74  ? 0.087   6.677   -28.099 1.00 39.62  ? 115 SER   A O   1 
ATOM   587  C  CB  . SER   A 1 74  ? -2.132  4.788   -26.435 1.00 33.52  ? 115 SER   A CB  1 
ATOM   588  O  OG  . SER   A 1 74  ? -2.475  3.542   -25.848 1.00 35.76  ? 115 SER   A OG  1 
ATOM   589  N  N   . LEU   A 1 75  ? -0.307  7.195   -25.934 1.00 38.59  ? 116 LEU   A N   1 
ATOM   590  C  CA  . LEU   A 1 75  ? -0.084  8.634   -26.063 1.00 39.53  ? 116 LEU   A CA  1 
ATOM   591  C  C   . LEU   A 1 75  ? 1.347   8.953   -25.645 1.00 41.95  ? 116 LEU   A C   1 
ATOM   592  O  O   . LEU   A 1 75  ? 1.625   9.429   -24.541 1.00 42.44  ? 116 LEU   A O   1 
ATOM   593  C  CB  . LEU   A 1 75  ? -1.120  9.398   -25.235 1.00 38.43  ? 116 LEU   A CB  1 
ATOM   594  C  CG  . LEU   A 1 75  ? -1.546  10.797  -25.698 1.00 43.20  ? 116 LEU   A CG  1 
ATOM   595  C  CD1 . LEU   A 1 75  ? -1.461  11.001  -27.204 1.00 39.59  ? 116 LEU   A CD1 1 
ATOM   596  C  CD2 . LEU   A 1 75  ? -2.961  11.106  -25.205 1.00 42.50  ? 116 LEU   A CD2 1 
ATOM   597  N  N   . GLN   A 1 76  ? 2.260   8.699   -26.571 1.00 40.96  ? 117 GLN   A N   1 
ATOM   598  C  CA  . GLN   A 1 76  ? 3.683   8.732   -26.290 1.00 44.48  ? 117 GLN   A CA  1 
ATOM   599  C  C   . GLN   A 1 76  ? 4.218   10.121  -26.585 1.00 39.25  ? 117 GLN   A C   1 
ATOM   600  O  O   . GLN   A 1 76  ? 4.136   10.570  -27.737 1.00 38.76  ? 117 GLN   A O   1 
ATOM   601  C  CB  . GLN   A 1 76  ? 4.398   7.724   -27.152 1.00 46.88  ? 117 GLN   A CB  1 
ATOM   602  C  CG  . GLN   A 1 76  ? 4.042   6.293   -26.815 1.00 51.61  ? 117 GLN   A CG  1 
ATOM   603  C  CD  . GLN   A 1 76  ? 4.708   5.302   -27.757 1.00 55.01  ? 117 GLN   A CD  1 
ATOM   604  O  OE1 . GLN   A 1 76  ? 5.049   5.640   -28.891 1.00 55.05  ? 117 GLN   A OE1 1 
ATOM   605  N  NE2 . GLN   A 1 76  ? 4.808   4.052   -27.326 1.00 58.10  ? 117 GLN   A NE2 1 
ATOM   606  N  N   . PRO   A 1 77  ? 4.799   10.818  -25.621 1.00 37.91  ? 118 PRO   A N   1 
ATOM   607  C  CA  . PRO   A 1 77  ? 5.403   12.113  -25.936 1.00 40.24  ? 118 PRO   A CA  1 
ATOM   608  C  C   . PRO   A 1 77  ? 6.761   11.944  -26.612 1.00 44.45  ? 118 PRO   A C   1 
ATOM   609  O  O   . PRO   A 1 77  ? 7.493   10.976  -26.382 1.00 46.24  ? 118 PRO   A O   1 
ATOM   610  C  CB  . PRO   A 1 77  ? 5.530   12.762  -24.557 1.00 41.57  ? 118 PRO   A CB  1 
ATOM   611  C  CG  . PRO   A 1 77  ? 5.766   11.574  -23.673 1.00 44.95  ? 118 PRO   A CG  1 
ATOM   612  C  CD  . PRO   A 1 77  ? 4.866   10.513  -24.177 1.00 38.32  ? 118 PRO   A CD  1 
ATOM   613  N  N   . CYS   A 1 78  ? 7.081   12.908  -27.479 1.00 41.25  ? 119 CYS   A N   1 
ATOM   614  C  CA  . CYS   A 1 78  ? 8.420   12.969  -28.053 1.00 46.01  ? 119 CYS   A CA  1 
ATOM   615  C  C   . CYS   A 1 78  ? 9.469   13.084  -26.966 1.00 46.73  ? 119 CYS   A C   1 
ATOM   616  O  O   . CYS   A 1 78  ? 10.561  12.515  -27.081 1.00 47.14  ? 119 CYS   A O   1 
ATOM   617  C  CB  . CYS   A 1 78  ? 8.544   14.162  -29.004 1.00 46.87  ? 119 CYS   A CB  1 
ATOM   618  S  SG  . CYS   A 1 78  ? 7.133   14.414  -30.085 1.00 52.77  ? 119 CYS   A SG  1 
ATOM   619  N  N   . VAL   A 1 79  ? 9.159   13.830  -25.913 1.00 45.81  ? 120 VAL   A N   1 
ATOM   620  C  CA  . VAL   A 1 79  ? 10.082  14.072  -24.816 1.00 49.41  ? 120 VAL   A CA  1 
ATOM   621  C  C   . VAL   A 1 79  ? 9.305   13.981  -23.512 1.00 47.30  ? 120 VAL   A C   1 
ATOM   622  O  O   . VAL   A 1 79  ? 8.206   14.533  -23.389 1.00 42.98  ? 120 VAL   A O   1 
ATOM   623  C  CB  . VAL   A 1 79  ? 10.777  15.445  -24.945 1.00 48.66  ? 120 VAL   A CB  1 
ATOM   624  C  CG1 . VAL   A 1 79  ? 11.786  15.634  -23.832 1.00 48.61  ? 120 VAL   A CG1 1 
ATOM   625  C  CG2 . VAL   A 1 79  ? 11.449  15.586  -26.304 1.00 48.62  ? 120 VAL   A CG2 1 
ATOM   626  N  N   . LYS   A 1 80  ? 9.871   13.268  -22.545 1.00 49.31  ? 121 LYS   A N   1 
ATOM   627  C  CA  . LYS   A 1 80  ? 9.360   13.234  -21.186 1.00 54.63  ? 121 LYS   A CA  1 
ATOM   628  C  C   . LYS   A 1 80  ? 10.452  13.750  -20.269 1.00 59.71  ? 121 LYS   A C   1 
ATOM   629  O  O   . LYS   A 1 80  ? 11.619  13.379  -20.413 1.00 64.19  ? 121 LYS   A O   1 
ATOM   630  C  CB  . LYS   A 1 80  ? 8.947   11.823  -20.764 1.00 58.38  ? 121 LYS   A CB  1 
ATOM   631  C  CG  . LYS   A 1 80  ? 8.544   10.971  -21.932 1.00 56.09  ? 121 LYS   A CG  1 
ATOM   632  C  CD  . LYS   A 1 80  ? 7.818   9.687   -21.546 1.00 58.77  ? 121 LYS   A CD  1 
ATOM   633  C  CE  . LYS   A 1 80  ? 8.744   8.564   -21.119 1.00 58.05  ? 121 LYS   A CE  1 
ATOM   634  N  NZ  . LYS   A 1 80  ? 8.009   7.602   -20.260 1.00 59.84  ? 121 LYS   A NZ  1 
ATOM   635  N  N   . LEU   A 1 81  ? 10.080  14.627  -19.343 1.00 60.52  ? 122 LEU   A N   1 
ATOM   636  C  CA  . LEU   A 1 81  ? 11.038  15.164  -18.391 1.00 64.63  ? 122 LEU   A CA  1 
ATOM   637  C  C   . LEU   A 1 81  ? 10.894  14.509  -17.021 1.00 71.29  ? 122 LEU   A C   1 
ATOM   638  O  O   . LEU   A 1 81  ? 11.301  15.089  -16.009 1.00 77.47  ? 122 LEU   A O   1 
ATOM   639  C  CB  . LEU   A 1 81  ? 10.897  16.685  -18.316 1.00 59.94  ? 122 LEU   A CB  1 
ATOM   640  C  CG  . LEU   A 1 81  ? 11.501  17.369  -19.556 1.00 59.78  ? 122 LEU   A CG  1 
ATOM   641  C  CD1 . LEU   A 1 81  ? 10.555  18.417  -20.130 1.00 57.41  ? 122 LEU   A CD1 1 
ATOM   642  C  CD2 . LEU   A 1 81  ? 12.863  17.984  -19.278 1.00 58.73  ? 122 LEU   A CD2 1 
ATOM   643  N  N   . THR   A 1 82  ? 10.329  13.298  -16.985 1.00 73.10  ? 123 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 82  ? 10.121  12.518  -15.770 1.00 74.81  ? 123 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 82  ? 11.339  12.513  -14.855 1.00 82.80  ? 123 THR   A C   1 
ATOM   646  O  O   . THR   A 1 82  ? 12.360  11.897  -15.172 1.00 83.20  ? 123 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 82  ? 9.747   11.072  -16.127 1.00 77.46  ? 123 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 82  ? 10.747  10.511  -16.990 1.00 77.04  ? 123 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 82  ? 8.393   11.015  -16.810 1.00 66.44  ? 123 THR   A CG2 1 
ATOM   650  N  N   . GLY   A 1 83  ? 11.241  13.199  -13.718 1.00 83.30  ? 124 GLY   A N   1 
ATOM   651  C  CA  . GLY   A 1 83  ? 12.259  13.087  -12.685 1.00 81.80  ? 124 GLY   A CA  1 
ATOM   652  C  C   . GLY   A 1 83  ? 13.602  13.685  -13.034 1.00 81.20  ? 124 GLY   A C   1 
ATOM   653  O  O   . GLY   A 1 83  ? 14.594  13.418  -12.346 1.00 78.06  ? 124 GLY   A O   1 
ATOM   654  N  N   . GLY   A 1 84  ? 13.662  14.507  -14.080 1.00 80.01  ? 198 GLY   A N   1 
ATOM   655  C  CA  . GLY   A 1 84  ? 14.910  15.059  -14.558 1.00 78.88  ? 198 GLY   A CA  1 
ATOM   656  C  C   . GLY   A 1 84  ? 15.635  14.202  -15.572 1.00 81.88  ? 198 GLY   A C   1 
ATOM   657  O  O   . GLY   A 1 84  ? 16.637  14.653  -16.135 1.00 78.40  ? 198 GLY   A O   1 
ATOM   658  N  N   . SER   A 1 85  ? 15.162  12.985  -15.827 1.00 83.43  ? 199 SER   A N   1 
ATOM   659  C  CA  . SER   A 1 85  ? 15.838  12.068  -16.743 1.00 79.11  ? 199 SER   A CA  1 
ATOM   660  C  C   . SER   A 1 85  ? 15.182  12.111  -18.124 1.00 79.37  ? 199 SER   A C   1 
ATOM   661  O  O   . SER   A 1 85  ? 14.472  11.195  -18.540 1.00 76.93  ? 199 SER   A O   1 
ATOM   662  C  CB  . SER   A 1 85  ? 15.824  10.661  -16.167 1.00 81.47  ? 199 SER   A CB  1 
ATOM   663  O  OG  . SER   A 1 85  ? 15.513  10.692  -14.782 1.00 74.95  ? 199 SER   A OG  1 
ATOM   664  N  N   . VAL   A 1 86  ? 15.462  13.203  -18.841 1.00 79.20  ? 200 VAL   A N   1 
ATOM   665  C  CA  . VAL   A 1 86  ? 14.776  13.496  -20.093 1.00 73.60  ? 200 VAL   A CA  1 
ATOM   666  C  C   . VAL   A 1 86  ? 14.953  12.331  -21.055 1.00 72.78  ? 200 VAL   A C   1 
ATOM   667  O  O   . VAL   A 1 86  ? 15.989  11.657  -21.046 1.00 76.63  ? 200 VAL   A O   1 
ATOM   668  C  CB  . VAL   A 1 86  ? 15.294  14.830  -20.664 1.00 72.36  ? 200 VAL   A CB  1 
ATOM   669  C  CG1 . VAL   A 1 86  ? 15.593  15.796  -19.527 1.00 70.29  ? 200 VAL   A CG1 1 
ATOM   670  C  CG2 . VAL   A 1 86  ? 16.548  14.627  -21.500 1.00 72.54  ? 200 VAL   A CG2 1 
ATOM   671  N  N   . ILE   A 1 87  ? 13.914  12.041  -21.838 1.00 68.49  ? 201 ILE   A N   1 
ATOM   672  C  CA  . ILE   A 1 87  ? 13.947  10.939  -22.792 1.00 67.68  ? 201 ILE   A CA  1 
ATOM   673  C  C   . ILE   A 1 87  ? 13.255  11.379  -24.079 1.00 64.17  ? 201 ILE   A C   1 
ATOM   674  O  O   . ILE   A 1 87  ? 12.150  11.934  -24.046 1.00 59.93  ? 201 ILE   A O   1 
ATOM   675  C  CB  . ILE   A 1 87  ? 13.329  9.647   -22.205 1.00 65.53  ? 201 ILE   A CB  1 
ATOM   676  C  CG1 . ILE   A 1 87  ? 13.920  8.409   -22.887 1.00 64.37  ? 201 ILE   A CG1 1 
ATOM   677  C  CG2 . ILE   A 1 87  ? 11.812  9.628   -22.278 1.00 65.60  ? 201 ILE   A CG2 1 
ATOM   678  C  CD1 . ILE   A 1 87  ? 14.138  7.246   -21.954 1.00 63.45  ? 201 ILE   A CD1 1 
ATOM   679  N  N   . LYS   A 1 88  ? 13.938  11.171  -25.209 1.00 63.44  ? 202 LYS   A N   1 
ATOM   680  C  CA  . LYS   A 1 88  ? 13.489  11.558  -26.544 1.00 57.33  ? 202 LYS   A CA  1 
ATOM   681  C  C   . LYS   A 1 88  ? 13.138  10.286  -27.310 1.00 58.86  ? 202 LYS   A C   1 
ATOM   682  O  O   . LYS   A 1 88  ? 14.035  9.552   -27.740 1.00 62.06  ? 202 LYS   A O   1 
ATOM   683  C  CB  . LYS   A 1 88  ? 14.583  12.325  -27.285 1.00 59.03  ? 202 LYS   A CB  1 
ATOM   684  C  CG  . LYS   A 1 88  ? 14.347  13.798  -27.575 1.00 59.99  ? 202 LYS   A CG  1 
ATOM   685  C  CD  . LYS   A 1 88  ? 15.372  14.248  -28.628 1.00 60.25  ? 202 LYS   A CD  1 
ATOM   686  C  CE  . LYS   A 1 88  ? 15.328  15.740  -28.939 1.00 59.62  ? 202 LYS   A CE  1 
ATOM   687  N  NZ  . LYS   A 1 88  ? 16.214  16.510  -28.028 1.00 60.23  ? 202 LYS   A NZ  1 
ATOM   688  N  N   . GLN   A 1 89  ? 11.852  10.029  -27.497 1.00 58.01  ? 203 GLN   A N   1 
ATOM   689  C  CA  . GLN   A 1 89  ? 11.412  8.782   -28.104 1.00 50.86  ? 203 GLN   A CA  1 
ATOM   690  C  C   . GLN   A 1 89  ? 10.529  9.074   -29.313 1.00 51.03  ? 203 GLN   A C   1 
ATOM   691  O  O   . GLN   A 1 89  ? 10.377  10.223  -29.746 1.00 56.45  ? 203 GLN   A O   1 
ATOM   692  C  CB  . GLN   A 1 89  ? 10.680  7.919   -27.070 1.00 52.36  ? 203 GLN   A CB  1 
ATOM   693  C  CG  . GLN   A 1 89  ? 9.307   8.452   -26.698 1.00 49.29  ? 203 GLN   A CG  1 
ATOM   694  C  CD  . GLN   A 1 89  ? 8.827   7.950   -25.350 1.00 56.22  ? 203 GLN   A CD  1 
ATOM   695  O  OE1 . GLN   A 1 89  ? 9.191   8.498   -24.307 1.00 61.18  ? 203 GLN   A OE1 1 
ATOM   696  N  NE2 . GLN   A 1 89  ? 8.019   6.894   -25.362 1.00 54.01  ? 203 GLN   A NE2 1 
ATOM   697  N  N   . ALA   A 1 90  ? 9.956   8.009   -29.863 1.00 50.96  ? 204 ALA   A N   1 
ATOM   698  C  CA  . ALA   A 1 90  ? 9.004   8.153   -30.950 1.00 50.15  ? 204 ALA   A CA  1 
ATOM   699  C  C   . ALA   A 1 90  ? 7.717   8.763   -30.426 1.00 50.60  ? 204 ALA   A C   1 
ATOM   700  O  O   . ALA   A 1 90  ? 7.240   8.410   -29.345 1.00 47.96  ? 204 ALA   A O   1 
ATOM   701  C  CB  . ALA   A 1 90  ? 8.699   6.802   -31.596 1.00 48.67  ? 204 ALA   A CB  1 
ATOM   702  N  N   . CYS   A 1 91  ? 7.140   9.669   -31.210 1.00 49.17  ? 205 CYS   A N   1 
ATOM   703  C  CA  . CYS   A 1 91  ? 5.843   10.267  -30.891 1.00 48.59  ? 205 CYS   A CA  1 
ATOM   704  C  C   . CYS   A 1 91  ? 5.012   10.408  -32.163 1.00 51.43  ? 205 CYS   A C   1 
ATOM   705  O  O   . CYS   A 1 91  ? 4.668   11.523  -32.563 1.00 52.07  ? 205 CYS   A O   1 
ATOM   706  C  CB  . CYS   A 1 91  ? 6.031   11.637  -30.239 1.00 48.55  ? 205 CYS   A CB  1 
ATOM   707  S  SG  . CYS   A 1 91  ? 7.148   12.717  -31.178 1.00 61.83  ? 205 CYS   A SG  1 
ATOM   708  N  N   . PRO   A 1 92  ? 4.655   9.297   -32.818 1.00 52.44  ? 206 PRO   A N   1 
ATOM   709  C  CA  . PRO   A 1 92  ? 3.803   9.417   -34.002 1.00 47.95  ? 206 PRO   A CA  1 
ATOM   710  C  C   . PRO   A 1 92  ? 2.422   9.938   -33.622 1.00 43.26  ? 206 PRO   A C   1 
ATOM   711  O  O   . PRO   A 1 92  ? 1.921   9.704   -32.519 1.00 38.89  ? 206 PRO   A O   1 
ATOM   712  C  CB  . PRO   A 1 92  ? 3.727   7.992   -34.550 1.00 44.42  ? 206 PRO   A CB  1 
ATOM   713  C  CG  . PRO   A 1 92  ? 4.455   7.130   -33.639 1.00 49.90  ? 206 PRO   A CG  1 
ATOM   714  C  CD  . PRO   A 1 92  ? 5.118   7.921   -32.593 1.00 51.29  ? 206 PRO   A CD  1 
ATOM   715  N  N   . LYS   A 1 93  ? 1.810   10.673  -34.548 1.00 42.85  ? 207 LYS   A N   1 
ATOM   716  C  CA  . LYS   A 1 93  ? 0.438   11.110  -34.339 1.00 45.06  ? 207 LYS   A CA  1 
ATOM   717  C  C   . LYS   A 1 93  ? -0.477  9.896   -34.440 1.00 39.73  ? 207 LYS   A C   1 
ATOM   718  O  O   . LYS   A 1 93  ? -0.306  9.047   -35.322 1.00 41.85  ? 207 LYS   A O   1 
ATOM   719  C  CB  . LYS   A 1 93  ? 0.064   12.166  -35.368 1.00 39.76  ? 207 LYS   A CB  1 
ATOM   720  C  CG  . LYS   A 1 93  ? 0.620   13.550  -35.054 1.00 44.00  ? 207 LYS   A CG  1 
ATOM   721  C  CD  . LYS   A 1 93  ? 0.002   14.180  -33.814 1.00 42.31  ? 207 LYS   A CD  1 
ATOM   722  C  CE  . LYS   A 1 93  ? 0.807   15.410  -33.405 1.00 37.32  ? 207 LYS   A CE  1 
ATOM   723  N  NZ  . LYS   A 1 93  ? 0.008   16.519  -32.820 1.00 41.01  ? 207 LYS   A NZ  1 
ATOM   724  N  N   . ILE   A 1 94  ? -1.424  9.791   -33.509 1.00 35.38  ? 208 ILE   A N   1 
ATOM   725  C  CA  . ILE   A 1 94  ? -2.214  8.581   -33.349 1.00 40.36  ? 208 ILE   A CA  1 
ATOM   726  C  C   . ILE   A 1 94  ? -3.680  8.906   -33.593 1.00 36.32  ? 208 ILE   A C   1 
ATOM   727  O  O   . ILE   A 1 94  ? -4.077  10.063  -33.699 1.00 30.97  ? 208 ILE   A O   1 
ATOM   728  C  CB  . ILE   A 1 94  ? -2.038  7.946   -31.956 1.00 39.93  ? 208 ILE   A CB  1 
ATOM   729  C  CG1 . ILE   A 1 94  ? -2.732  8.832   -30.908 1.00 35.71  ? 208 ILE   A CG1 1 
ATOM   730  C  CG2 . ILE   A 1 94  ? -0.567  7.759   -31.628 1.00 40.85  ? 208 ILE   A CG2 1 
ATOM   731  C  CD1 . ILE   A 1 94  ? -2.324  8.548   -29.490 1.00 39.04  ? 208 ILE   A CD1 1 
ATOM   732  N  N   . SER   A 1 95  ? -4.480  7.849   -33.678 1.00 36.62  ? 209 SER   A N   1 
ATOM   733  C  CA  . SER   A 1 95  ? -5.926  7.949   -33.604 1.00 31.62  ? 209 SER   A CA  1 
ATOM   734  C  C   . SER   A 1 95  ? -6.345  7.736   -32.155 1.00 33.66  ? 209 SER   A C   1 
ATOM   735  O  O   . SER   A 1 95  ? -5.956  6.741   -31.538 1.00 30.56  ? 209 SER   A O   1 
ATOM   736  C  CB  . SER   A 1 95  ? -6.581  6.917   -34.519 1.00 30.86  ? 209 SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 95  ? -7.955  6.770   -34.214 1.00 42.85  ? 209 SER   A OG  1 
ATOM   738  N  N   . PHE   A 1 96  ? -7.128  8.672   -31.614 1.00 29.33  ? 210 PHE   A N   1 
ATOM   739  C  CA  . PHE   A 1 96  ? -7.436  8.711   -30.185 1.00 27.48  ? 210 PHE   A CA  1 
ATOM   740  C  C   . PHE   A 1 96  ? -8.896  9.095   -30.014 1.00 32.00  ? 210 PHE   A C   1 
ATOM   741  O  O   . PHE   A 1 96  ? -9.285  10.209  -30.370 1.00 35.63  ? 210 PHE   A O   1 
ATOM   742  C  CB  . PHE   A 1 96  ? -6.524  9.713   -29.462 1.00 29.84  ? 210 PHE   A CB  1 
ATOM   743  C  CG  . PHE   A 1 96  ? -6.732  9.784   -27.970 1.00 30.46  ? 210 PHE   A CG  1 
ATOM   744  C  CD1 . PHE   A 1 96  ? -7.759  10.542  -27.427 1.00 30.28  ? 210 PHE   A CD1 1 
ATOM   745  C  CD2 . PHE   A 1 96  ? -5.875  9.122   -27.107 1.00 29.42  ? 210 PHE   A CD2 1 
ATOM   746  C  CE1 . PHE   A 1 96  ? -7.938  10.614  -26.053 1.00 29.19  ? 210 PHE   A CE1 1 
ATOM   747  C  CE2 . PHE   A 1 96  ? -6.048  9.194   -25.735 1.00 30.47  ? 210 PHE   A CE2 1 
ATOM   748  C  CZ  . PHE   A 1 96  ? -7.079  9.940   -25.209 1.00 29.10  ? 210 PHE   A CZ  1 
ATOM   749  N  N   . ASP   A 1 97  ? -9.696  8.187   -29.450 1.00 30.73  ? 211 ASP   A N   1 
ATOM   750  C  CA  . ASP   A 1 97  ? -11.119 8.425   -29.214 1.00 33.81  ? 211 ASP   A CA  1 
ATOM   751  C  C   . ASP   A 1 97  ? -11.681 7.442   -28.201 1.00 33.95  ? 211 ASP   A C   1 
ATOM   752  O  O   . ASP   A 1 97  ? -11.923 6.289   -28.565 1.00 33.10  ? 211 ASP   A O   1 
ATOM   753  C  CB  . ASP   A 1 97  ? -11.908 8.316   -30.511 1.00 34.73  ? 211 ASP   A CB  1 
ATOM   754  C  CG  . ASP   A 1 97  ? -13.387 8.557   -30.303 1.00 35.58  ? 211 ASP   A CG  1 
ATOM   755  O  OD1 . ASP   A 1 97  ? -13.736 9.409   -29.462 1.00 34.68  ? 211 ASP   A OD1 1 
ATOM   756  O  OD2 . ASP   A 1 97  ? -14.206 7.896   -30.986 1.00 46.27  ? 211 ASP   A OD2 1 
ATOM   757  N  N   . PRO   A 1 98  ? -11.858 7.828   -26.935 1.00 32.85  ? 212 PRO   A N   1 
ATOM   758  C  CA  . PRO   A 1 98  ? -12.095 6.836   -25.871 1.00 32.17  ? 212 PRO   A CA  1 
ATOM   759  C  C   . PRO   A 1 98  ? -13.265 5.908   -26.176 1.00 31.61  ? 212 PRO   A C   1 
ATOM   760  O  O   . PRO   A 1 98  ? -14.274 6.328   -26.742 1.00 34.21  ? 212 PRO   A O   1 
ATOM   761  C  CB  . PRO   A 1 98  ? -12.376 7.703   -24.639 1.00 29.54  ? 212 PRO   A CB  1 
ATOM   762  C  CG  . PRO   A 1 98  ? -11.667 9.005   -24.932 1.00 29.51  ? 212 PRO   A CG  1 
ATOM   763  C  CD  . PRO   A 1 98  ? -11.793 9.205   -26.414 1.00 31.68  ? 212 PRO   A CD  1 
ATOM   764  N  N   . ILE   A 1 99  ? -13.117 4.639   -25.804 1.00 32.23  ? 213 ILE   A N   1 
ATOM   765  C  CA  . ILE   A 1 99  ? -14.180 3.641   -25.932 1.00 30.23  ? 213 ILE   A CA  1 
ATOM   766  C  C   . ILE   A 1 99  ? -14.565 3.193   -24.523 1.00 27.62  ? 213 ILE   A C   1 
ATOM   767  O  O   . ILE   A 1 99  ? -13.784 3.342   -23.572 1.00 26.86  ? 213 ILE   A O   1 
ATOM   768  C  CB  . ILE   A 1 99  ? -13.753 2.432   -26.797 1.00 29.12  ? 213 ILE   A CB  1 
ATOM   769  C  CG1 . ILE   A 1 99  ? -12.631 1.628   -26.121 1.00 33.79  ? 213 ILE   A CG1 1 
ATOM   770  C  CG2 . ILE   A 1 99  ? -13.349 2.879   -28.182 1.00 35.55  ? 213 ILE   A CG2 1 
ATOM   771  C  CD1 . ILE   A 1 99  ? -12.146 0.452   -26.968 1.00 32.49  ? 213 ILE   A CD1 1 
ATOM   772  N  N   . PRO   A 1 100 ? -15.758 2.628   -24.366 1.00 33.58  ? 214 PRO   A N   1 
ATOM   773  C  CA  . PRO   A 1 100 ? -16.159 2.112   -23.050 1.00 30.40  ? 214 PRO   A CA  1 
ATOM   774  C  C   . PRO   A 1 100 ? -15.333 0.908   -22.607 1.00 30.83  ? 214 PRO   A C   1 
ATOM   775  O  O   . PRO   A 1 100 ? -15.062 -0.009  -23.385 1.00 31.25  ? 214 PRO   A O   1 
ATOM   776  C  CB  . PRO   A 1 100 ? -17.631 1.737   -23.266 1.00 35.19  ? 214 PRO   A CB  1 
ATOM   777  C  CG  . PRO   A 1 100 ? -18.052 2.567   -24.441 1.00 34.61  ? 214 PRO   A CG  1 
ATOM   778  C  CD  . PRO   A 1 100 ? -16.870 2.577   -25.324 1.00 33.97  ? 214 PRO   A CD  1 
ATOM   779  N  N   . ILE   A 1 101 ? -14.936 0.926   -21.334 1.00 28.87  ? 215 ILE   A N   1 
ATOM   780  C  CA  . ILE   A 1 101 ? -14.236 -0.173  -20.682 1.00 31.54  ? 215 ILE   A CA  1 
ATOM   781  C  C   . ILE   A 1 101 ? -15.145 -0.696  -19.580 1.00 29.66  ? 215 ILE   A C   1 
ATOM   782  O  O   . ILE   A 1 101 ? -15.765 0.092   -18.859 1.00 32.93  ? 215 ILE   A O   1 
ATOM   783  C  CB  . ILE   A 1 101 ? -12.877 0.274   -20.093 1.00 30.29  ? 215 ILE   A CB  1 
ATOM   784  C  CG1 . ILE   A 1 101 ? -11.975 0.955   -21.134 1.00 28.24  ? 215 ILE   A CG1 1 
ATOM   785  C  CG2 . ILE   A 1 101 ? -12.157 -0.911  -19.483 1.00 30.97  ? 215 ILE   A CG2 1 
ATOM   786  C  CD1 . ILE   A 1 101 ? -11.951 0.294   -22.499 1.00 33.29  ? 215 ILE   A CD1 1 
ATOM   787  N  N   . HIS   A 1 102 ? -15.239 -2.015  -19.461 1.00 34.54  ? 216 HIS   A N   1 
ATOM   788  C  CA  . HIS   A 1 102 ? -15.996 -2.653  -18.396 1.00 34.41  ? 216 HIS   A CA  1 
ATOM   789  C  C   . HIS   A 1 102 ? -15.023 -3.233  -17.388 1.00 30.88  ? 216 HIS   A C   1 
ATOM   790  O  O   . HIS   A 1 102 ? -14.008 -3.813  -17.772 1.00 35.63  ? 216 HIS   A O   1 
ATOM   791  C  CB  . HIS   A 1 102 ? -16.879 -3.781  -18.925 1.00 31.70  ? 216 HIS   A CB  1 
ATOM   792  C  CG  . HIS   A 1 102 ? -17.947 -3.335  -19.866 1.00 34.01  ? 216 HIS   A CG  1 
ATOM   793  N  ND1 . HIS   A 1 102 ? -19.272 -3.274  -19.503 1.00 32.79  ? 216 HIS   A ND1 1 
ATOM   794  C  CD2 . HIS   A 1 102 ? -17.899 -2.979  -21.171 1.00 34.72  ? 216 HIS   A CD2 1 
ATOM   795  C  CE1 . HIS   A 1 102 ? -19.993 -2.877  -20.536 1.00 36.53  ? 216 HIS   A CE1 1 
ATOM   796  N  NE2 . HIS   A 1 102 ? -19.183 -2.690  -21.562 1.00 34.53  ? 216 HIS   A NE2 1 
ATOM   797  N  N   . TYR   A 1 103 ? -15.334 -3.093  -16.107 1.00 31.48  ? 217 TYR   A N   1 
ATOM   798  C  CA  . TYR   A 1 103 ? -14.533 -3.708  -15.059 1.00 32.82  ? 217 TYR   A CA  1 
ATOM   799  C  C   . TYR   A 1 103 ? -15.279 -4.885  -14.455 1.00 37.91  ? 217 TYR   A C   1 
ATOM   800  O  O   . TYR   A 1 103 ? -16.449 -4.765  -14.080 1.00 34.97  ? 217 TYR   A O   1 
ATOM   801  C  CB  . TYR   A 1 103 ? -14.122 -2.678  -14.007 1.00 31.55  ? 217 TYR   A CB  1 
ATOM   802  C  CG  . TYR   A 1 103 ? -13.029 -1.835  -14.588 1.00 35.02  ? 217 TYR   A CG  1 
ATOM   803  C  CD1 . TYR   A 1 103 ? -11.717 -2.275  -14.551 1.00 32.99  ? 217 TYR   A CD1 1 
ATOM   804  C  CD2 . TYR   A 1 103 ? -13.312 -0.664  -15.274 1.00 31.88  ? 217 TYR   A CD2 1 
ATOM   805  C  CE1 . TYR   A 1 103 ? -10.711 -1.552  -15.115 1.00 34.11  ? 217 TYR   A CE1 1 
ATOM   806  C  CE2 . TYR   A 1 103 ? -12.301 0.075   -15.850 1.00 25.95  ? 217 TYR   A CE2 1 
ATOM   807  C  CZ  . TYR   A 1 103 ? -11.003 -0.378  -15.767 1.00 30.02  ? 217 TYR   A CZ  1 
ATOM   808  O  OH  . TYR   A 1 103 ? -9.982  0.340   -16.336 1.00 31.62  ? 217 TYR   A OH  1 
ATOM   809  N  N   . CYS   A 1 104 ? -14.600 -6.030  -14.404 1.00 34.99  ? 218 CYS   A N   1 
ATOM   810  C  CA  . CYS   A 1 104 ? -15.210 -7.307  -14.072 1.00 40.28  ? 218 CYS   A CA  1 
ATOM   811  C  C   . CYS   A 1 104 ? -14.397 -7.999  -12.988 1.00 38.63  ? 218 CYS   A C   1 
ATOM   812  O  O   . CYS   A 1 104 ? -13.170 -7.880  -12.940 1.00 37.17  ? 218 CYS   A O   1 
ATOM   813  C  CB  . CYS   A 1 104 ? -15.287 -8.223  -15.297 1.00 37.84  ? 218 CYS   A CB  1 
ATOM   814  S  SG  . CYS   A 1 104 ? -15.986 -7.485  -16.787 1.00 40.20  ? 218 CYS   A SG  1 
ATOM   815  N  N   . THR   A 1 105 ? -15.095 -8.745  -12.126 1.00 37.32  ? 219 THR   A N   1 
ATOM   816  C  CA  . THR   A 1 105 ? -14.521 -9.524  -11.036 1.00 40.10  ? 219 THR   A CA  1 
ATOM   817  C  C   . THR   A 1 105 ? -14.155 -10.931 -11.503 1.00 40.86  ? 219 THR   A C   1 
ATOM   818  O  O   . THR   A 1 105 ? -14.768 -11.463 -12.435 1.00 39.68  ? 219 THR   A O   1 
ATOM   819  C  CB  . THR   A 1 105 ? -15.506 -9.614  -9.869  1.00 38.33  ? 219 THR   A CB  1 
ATOM   820  O  OG1 . THR   A 1 105 ? -16.835 -9.803  -10.365 1.00 38.48  ? 219 THR   A OG1 1 
ATOM   821  C  CG2 . THR   A 1 105 ? -15.457 -8.365  -9.022  1.00 41.41  ? 219 THR   A CG2 1 
ATOM   822  N  N   . PRO   A 1 106 ? -13.148 -11.547 -10.895 1.00 39.17  ? 220 PRO   A N   1 
ATOM   823  C  CA  . PRO   A 1 106 ? -12.874 -12.962 -11.149 1.00 41.38  ? 220 PRO   A CA  1 
ATOM   824  C  C   . PRO   A 1 106 ? -13.888 -13.832 -10.415 1.00 43.05  ? 220 PRO   A C   1 
ATOM   825  O  O   . PRO   A 1 106 ? -14.726 -13.353 -9.653  1.00 41.29  ? 220 PRO   A O   1 
ATOM   826  C  CB  . PRO   A 1 106 ? -11.459 -13.164 -10.603 1.00 41.42  ? 220 PRO   A CB  1 
ATOM   827  C  CG  . PRO   A 1 106 ? -11.261 -12.072 -9.613  1.00 42.13  ? 220 PRO   A CG  1 
ATOM   828  C  CD  . PRO   A 1 106 ? -12.157 -10.930 -9.999  1.00 39.47  ? 220 PRO   A CD  1 
ATOM   829  N  N   . ALA   A 1 107 ? -13.803 -15.135 -10.669 1.00 45.53  ? 221 ALA   A N   1 
ATOM   830  C  CA  . ALA   A 1 107 ? -14.651 -16.081 -9.961  1.00 43.06  ? 221 ALA   A CA  1 
ATOM   831  C  C   . ALA   A 1 107 ? -14.418 -15.973 -8.459  1.00 40.72  ? 221 ALA   A C   1 
ATOM   832  O  O   . ALA   A 1 107 ? -13.286 -15.805 -7.999  1.00 42.56  ? 221 ALA   A O   1 
ATOM   833  C  CB  . ALA   A 1 107 ? -14.377 -17.503 -10.443 1.00 48.17  ? 221 ALA   A CB  1 
ATOM   834  N  N   . GLY   A 1 108 ? -15.501 -16.069 -7.689  1.00 42.45  ? 222 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 108 ? -15.439 -15.945 -6.246  1.00 38.52  ? 222 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 108 ? -15.700 -14.549 -5.722  1.00 44.14  ? 222 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 108 ? -15.731 -14.356 -4.500  1.00 44.78  ? 222 GLY   A O   1 
ATOM   838  N  N   . TYR   A 1 109 ? -15.887 -13.576 -6.610  1.00 42.62  ? 223 TYR   A N   1 
ATOM   839  C  CA  . TYR   A 1 109 ? -16.186 -12.201 -6.244  1.00 44.04  ? 223 TYR   A CA  1 
ATOM   840  C  C   . TYR   A 1 109 ? -17.311 -11.722 -7.147  1.00 42.22  ? 223 TYR   A C   1 
ATOM   841  O  O   . TYR   A 1 109 ? -17.531 -12.272 -8.225  1.00 38.86  ? 223 TYR   A O   1 
ATOM   842  C  CB  . TYR   A 1 109 ? -14.966 -11.283 -6.419  1.00 41.39  ? 223 TYR   A CB  1 
ATOM   843  C  CG  . TYR   A 1 109 ? -13.791 -11.621 -5.533  1.00 41.92  ? 223 TYR   A CG  1 
ATOM   844  C  CD1 . TYR   A 1 109 ? -12.912 -12.631 -5.891  1.00 41.35  ? 223 TYR   A CD1 1 
ATOM   845  C  CD2 . TYR   A 1 109 ? -13.544 -10.921 -4.361  1.00 45.45  ? 223 TYR   A CD2 1 
ATOM   846  C  CE1 . TYR   A 1 109 ? -11.834 -12.956 -5.100  1.00 41.22  ? 223 TYR   A CE1 1 
ATOM   847  C  CE2 . TYR   A 1 109 ? -12.462 -11.237 -3.558  1.00 50.81  ? 223 TYR   A CE2 1 
ATOM   848  C  CZ  . TYR   A 1 109 ? -11.611 -12.259 -3.935  1.00 42.45  ? 223 TYR   A CZ  1 
ATOM   849  O  OH  . TYR   A 1 109 ? -10.530 -12.583 -3.148  1.00 46.92  ? 223 TYR   A OH  1 
ATOM   850  N  N   . VAL   A 1 110 ? -18.020 -10.681 -6.723  1.00 38.24  ? 224 VAL   A N   1 
ATOM   851  C  CA  . VAL   A 1 110 ? -18.982 -10.010 -7.594  1.00 42.74  ? 224 VAL   A CA  1 
ATOM   852  C  C   . VAL   A 1 110 ? -18.934 -8.508  -7.344  1.00 40.90  ? 224 VAL   A C   1 
ATOM   853  O  O   . VAL   A 1 110 ? -18.323 -8.023  -6.391  1.00 39.09  ? 224 VAL   A O   1 
ATOM   854  C  CB  . VAL   A 1 110 ? -20.440 -10.515 -7.427  1.00 40.95  ? 224 VAL   A CB  1 
ATOM   855  C  CG1 . VAL   A 1 110 ? -20.579 -11.972 -7.828  1.00 43.43  ? 224 VAL   A CG1 1 
ATOM   856  C  CG2 . VAL   A 1 110 ? -20.951 -10.289 -6.018  1.00 41.99  ? 224 VAL   A CG2 1 
ATOM   857  N  N   . ILE   A 1 111 ? -19.595 -7.768  -8.223  1.00 41.09  ? 225 ILE   A N   1 
ATOM   858  C  CA  . ILE   A 1 111 ? -19.685 -6.319  -8.145  1.00 38.45  ? 225 ILE   A CA  1 
ATOM   859  C  C   . ILE   A 1 111 ? -21.082 -5.964  -7.656  1.00 37.66  ? 225 ILE   A C   1 
ATOM   860  O  O   . ILE   A 1 111 ? -22.085 -6.380  -8.251  1.00 44.84  ? 225 ILE   A O   1 
ATOM   861  C  CB  . ILE   A 1 111 ? -19.391 -5.673  -9.507  1.00 37.41  ? 225 ILE   A CB  1 
ATOM   862  C  CG1 . ILE   A 1 111 ? -17.991 -6.064  -9.985  1.00 39.13  ? 225 ILE   A CG1 1 
ATOM   863  C  CG2 . ILE   A 1 111 ? -19.547 -4.168  -9.427  1.00 35.05  ? 225 ILE   A CG2 1 
ATOM   864  C  CD1 . ILE   A 1 111 ? -17.616 -5.471  -11.303 1.00 36.99  ? 225 ILE   A CD1 1 
ATOM   865  N  N   . LEU   A 1 112 ? -21.152 -5.204  -6.570  1.00 39.89  ? 226 LEU   A N   1 
ATOM   866  C  CA  . LEU   A 1 112 ? -22.424 -4.737  -6.043  1.00 38.38  ? 226 LEU   A CA  1 
ATOM   867  C  C   . LEU   A 1 112 ? -22.710 -3.358  -6.618  1.00 40.91  ? 226 LEU   A C   1 
ATOM   868  O  O   . LEU   A 1 112 ? -21.849 -2.474  -6.583  1.00 37.90  ? 226 LEU   A O   1 
ATOM   869  C  CB  . LEU   A 1 112 ? -22.392 -4.695  -4.516  1.00 41.92  ? 226 LEU   A CB  1 
ATOM   870  C  CG  . LEU   A 1 112 ? -22.274 -6.038  -3.781  1.00 43.29  ? 226 LEU   A CG  1 
ATOM   871  C  CD1 . LEU   A 1 112 ? -22.955 -5.978  -2.419  1.00 47.12  ? 226 LEU   A CD1 1 
ATOM   872  C  CD2 . LEU   A 1 112 ? -22.813 -7.208  -4.609  1.00 46.34  ? 226 LEU   A CD2 1 
ATOM   873  N  N   . LYS   A 1 113 ? -23.909 -3.184  -7.163  1.00 41.72  ? 227 LYS   A N   1 
ATOM   874  C  CA  . LYS   A 1 113 ? -24.269 -1.986  -7.905  1.00 41.34  ? 227 LYS   A CA  1 
ATOM   875  C  C   . LYS   A 1 113 ? -25.387 -1.257  -7.179  1.00 43.10  ? 227 LYS   A C   1 
ATOM   876  O  O   . LYS   A 1 113 ? -26.409 -1.863  -6.838  1.00 45.31  ? 227 LYS   A O   1 
ATOM   877  C  CB  . LYS   A 1 113 ? -24.698 -2.346  -9.327  1.00 43.87  ? 227 LYS   A CB  1 
ATOM   878  C  CG  . LYS   A 1 113 ? -24.898 -1.174  -10.259 1.00 42.97  ? 227 LYS   A CG  1 
ATOM   879  C  CD  . LYS   A 1 113 ? -25.547 -1.656  -11.555 1.00 44.38  ? 227 LYS   A CD  1 
ATOM   880  C  CE  . LYS   A 1 113 ? -25.944 -0.502  -12.462 1.00 41.71  ? 227 LYS   A CE  1 
ATOM   881  N  NZ  . LYS   A 1 113 ? -26.293 -1.018  -13.820 1.00 39.20  ? 227 LYS   A NZ  1 
ATOM   882  N  N   . CYS   A 1 114 ? -25.192 0.039   -6.945  1.00 38.98  ? 228 CYS   A N   1 
ATOM   883  C  CA  . CYS   A 1 114 ? -26.182 0.866   -6.266  1.00 43.77  ? 228 CYS   A CA  1 
ATOM   884  C  C   . CYS   A 1 114 ? -27.119 1.471   -7.302  1.00 45.94  ? 228 CYS   A C   1 
ATOM   885  O  O   . CYS   A 1 114 ? -26.702 2.290   -8.127  1.00 44.81  ? 228 CYS   A O   1 
ATOM   886  C  CB  . CYS   A 1 114 ? -25.519 1.963   -5.446  1.00 42.78  ? 228 CYS   A CB  1 
ATOM   887  S  SG  . CYS   A 1 114 ? -26.753 2.926   -4.601  1.00 55.07  ? 228 CYS   A SG  1 
ATOM   888  N  N   . ASN   A 1 115 ? -28.387 1.073   -7.254  1.00 44.34  ? 229 ASN   A N   1 
ATOM   889  C  CA  . ASN   A 1 115 ? -29.383 1.519   -8.215  1.00 46.55  ? 229 ASN   A CA  1 
ATOM   890  C  C   . ASN   A 1 115 ? -30.298 2.601   -7.659  1.00 45.04  ? 229 ASN   A C   1 
ATOM   891  O  O   . ASN   A 1 115 ? -31.236 3.010   -8.348  1.00 48.69  ? 229 ASN   A O   1 
ATOM   892  C  CB  . ASN   A 1 115 ? -30.213 0.329   -8.695  1.00 49.46  ? 229 ASN   A CB  1 
ATOM   893  C  CG  . ASN   A 1 115 ? -29.355 -0.809  -9.200  1.00 46.83  ? 229 ASN   A CG  1 
ATOM   894  O  OD1 . ASN   A 1 115 ? -28.843 -0.768  -10.320 1.00 46.66  ? 229 ASN   A OD1 1 
ATOM   895  N  ND2 . ASN   A 1 115 ? -29.183 -1.833  -8.370  1.00 48.11  ? 229 ASN   A ND2 1 
ATOM   896  N  N   . ASP   A 1 116 ? -30.047 3.076   -6.438  1.00 46.69  ? 230 ASP   A N   1 
ATOM   897  C  CA  . ASP   A 1 116 ? -30.740 4.260   -5.943  1.00 46.44  ? 230 ASP   A CA  1 
ATOM   898  C  C   . ASP   A 1 116 ? -30.459 5.443   -6.862  1.00 45.36  ? 230 ASP   A C   1 
ATOM   899  O  O   . ASP   A 1 116 ? -29.302 5.824   -7.067  1.00 42.76  ? 230 ASP   A O   1 
ATOM   900  C  CB  . ASP   A 1 116 ? -30.303 4.594   -4.515  1.00 45.24  ? 230 ASP   A CB  1 
ATOM   901  C  CG  . ASP   A 1 116 ? -30.785 3.579   -3.496  1.00 49.23  ? 230 ASP   A CG  1 
ATOM   902  O  OD1 . ASP   A 1 116 ? -31.588 2.700   -3.865  1.00 49.47  ? 230 ASP   A OD1 1 
ATOM   903  O  OD2 . ASP   A 1 116 ? -30.364 3.656   -2.320  1.00 51.31  ? 230 ASP   A OD2 1 
ATOM   904  N  N   . LYS   A 1 117 ? -31.523 6.029   -7.421  1.00 47.61  ? 231 LYS   A N   1 
ATOM   905  C  CA  . LYS   A 1 117 ? -31.336 7.100   -8.394  1.00 49.36  ? 231 LYS   A CA  1 
ATOM   906  C  C   . LYS   A 1 117 ? -30.819 8.385   -7.760  1.00 45.09  ? 231 LYS   A C   1 
ATOM   907  O  O   . LYS   A 1 117 ? -30.297 9.245   -8.479  1.00 49.74  ? 231 LYS   A O   1 
ATOM   908  C  CB  . LYS   A 1 117 ? -32.634 7.370   -9.158  1.00 52.79  ? 231 LYS   A CB  1 
ATOM   909  C  CG  . LYS   A 1 117 ? -33.069 6.215   -10.048 1.00 56.98  ? 231 LYS   A CG  1 
ATOM   910  C  CD  . LYS   A 1 117 ? -34.371 6.516   -10.763 1.00 55.38  ? 231 LYS   A CD  1 
ATOM   911  C  CE  . LYS   A 1 117 ? -34.847 5.314   -11.554 1.00 55.88  ? 231 LYS   A CE  1 
ATOM   912  N  NZ  . LYS   A 1 117 ? -33.910 4.975   -12.655 1.00 63.11  ? 231 LYS   A NZ  1 
ATOM   913  N  N   . ASN   A 1 118 ? -30.932 8.535   -6.440  1.00 41.63  ? 232 ASN   A N   1 
ATOM   914  C  CA  . ASN   A 1 118 ? -30.426 9.719   -5.754  1.00 46.70  ? 232 ASN   A CA  1 
ATOM   915  C  C   . ASN   A 1 118 ? -29.127 9.446   -5.010  1.00 43.37  ? 232 ASN   A C   1 
ATOM   916  O  O   . ASN   A 1 118 ? -28.682 10.295  -4.230  1.00 40.21  ? 232 ASN   A O   1 
ATOM   917  C  CB  . ASN   A 1 118 ? -31.462 10.260  -4.769  1.00 49.98  ? 232 ASN   A CB  1 
ATOM   918  C  CG  . ASN   A 1 118 ? -32.031 9.181   -3.875  1.00 50.46  ? 232 ASN   A CG  1 
ATOM   919  O  OD1 . ASN   A 1 118 ? -31.632 8.019   -3.955  1.00 46.73  ? 232 ASN   A OD1 1 
ATOM   920  N  ND2 . ASN   A 1 118 ? -32.949 9.566   -2.991  1.00 53.88  ? 232 ASN   A ND2 1 
ATOM   921  N  N   . PHE   A 1 119 ? -28.526 8.277   -5.213  1.00 43.54  ? 233 PHE   A N   1 
ATOM   922  C  CA  . PHE   A 1 119 ? -27.333 7.906   -4.466  1.00 40.21  ? 233 PHE   A CA  1 
ATOM   923  C  C   . PHE   A 1 119 ? -26.222 8.918   -4.712  1.00 42.58  ? 233 PHE   A C   1 
ATOM   924  O  O   . PHE   A 1 119 ? -25.889 9.228   -5.859  1.00 35.32  ? 233 PHE   A O   1 
ATOM   925  C  CB  . PHE   A 1 119 ? -26.891 6.504   -4.865  1.00 40.52  ? 233 PHE   A CB  1 
ATOM   926  C  CG  . PHE   A 1 119 ? -25.614 6.057   -4.215  1.00 40.02  ? 233 PHE   A CG  1 
ATOM   927  C  CD1 . PHE   A 1 119 ? -25.489 6.051   -2.838  1.00 41.26  ? 233 PHE   A CD1 1 
ATOM   928  C  CD2 . PHE   A 1 119 ? -24.556 5.596   -4.980  1.00 40.00  ? 233 PHE   A CD2 1 
ATOM   929  C  CE1 . PHE   A 1 119 ? -24.324 5.628   -2.237  1.00 41.85  ? 233 PHE   A CE1 1 
ATOM   930  C  CE2 . PHE   A 1 119 ? -23.393 5.165   -4.382  1.00 42.78  ? 233 PHE   A CE2 1 
ATOM   931  C  CZ  . PHE   A 1 119 ? -23.283 5.172   -3.011  1.00 44.84  ? 233 PHE   A CZ  1 
ATOM   932  N  N   . ASN   A 1 120 ? -25.668 9.454   -3.628  1.00 34.62  ? 234 ASN   A N   1 
ATOM   933  C  CA  . ASN   A 1 120 ? -24.671 10.509  -3.716  1.00 38.87  ? 234 ASN   A CA  1 
ATOM   934  C  C   . ASN   A 1 120 ? -23.240 9.997   -3.691  1.00 40.78  ? 234 ASN   A C   1 
ATOM   935  O  O   . ASN   A 1 120 ? -22.306 10.801  -3.791  1.00 36.03  ? 234 ASN   A O   1 
ATOM   936  C  CB  . ASN   A 1 120 ? -24.897 11.535  -2.597  1.00 39.20  ? 234 ASN   A CB  1 
ATOM   937  C  CG  . ASN   A 1 120 ? -24.514 11.023  -1.215  1.00 41.54  ? 234 ASN   A CG  1 
ATOM   938  O  OD1 . ASN   A 1 120 ? -23.743 10.075  -1.056  1.00 41.26  ? 234 ASN   A OD1 1 
ATOM   939  N  ND2 . ASN   A 1 120 ? -25.055 11.669  -0.200  1.00 42.53  ? 234 ASN   A ND2 1 
ATOM   940  N  N   . GLY   A 1 121 ? -23.044 8.693   -3.516  1.00 40.39  ? 235 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? -21.734 8.084   -3.583  1.00 38.52  ? 235 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? -21.237 7.471   -2.288  1.00 39.62  ? 235 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? -20.431 6.533   -2.338  1.00 38.75  ? 235 GLY   A O   1 
ATOM   944  N  N   . THR   A 1 122 ? -21.688 7.958   -1.133  1.00 41.46  ? 236 THR   A N   1 
ATOM   945  C  CA  . THR   A 1 122 ? -21.239 7.426   0.147   1.00 43.35  ? 236 THR   A CA  1 
ATOM   946  C  C   . THR   A 1 122 ? -22.418 7.004   1.009   1.00 41.93  ? 236 THR   A C   1 
ATOM   947  O  O   . THR   A 1 122 ? -23.465 7.660   1.023   1.00 42.51  ? 236 THR   A O   1 
ATOM   948  C  CB  . THR   A 1 122 ? -20.384 8.449   0.918   1.00 44.95  ? 236 THR   A CB  1 
ATOM   949  O  OG1 . THR   A 1 122 ? -21.234 9.277   1.722   1.00 49.32  ? 236 THR   A OG1 1 
ATOM   950  C  CG2 . THR   A 1 122 ? -19.573 9.308   -0.019  1.00 39.62  ? 236 THR   A CG2 1 
ATOM   951  N  N   . GLY   A 1 123 ? -22.231 5.905   1.735   1.00 41.12  ? 237 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 123 ? -23.201 5.460   2.702   1.00 43.05  ? 237 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 123 ? -24.136 4.397   2.171   1.00 44.38  ? 237 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 123 ? -23.816 3.652   1.235   1.00 43.62  ? 237 GLY   A O   1 
ATOM   955  N  N   . PRO   A 1 124 ? -25.329 4.327   2.757   1.00 46.52  ? 238 PRO   A N   1 
ATOM   956  C  CA  . PRO   A 1 124 ? -26.230 3.211   2.461   1.00 46.16  ? 238 PRO   A CA  1 
ATOM   957  C  C   . PRO   A 1 124 ? -26.912 3.338   1.111   1.00 44.78  ? 238 PRO   A C   1 
ATOM   958  O  O   . PRO   A 1 124 ? -27.328 4.420   0.692   1.00 47.83  ? 238 PRO   A O   1 
ATOM   959  C  CB  . PRO   A 1 124 ? -27.244 3.257   3.610   1.00 47.72  ? 238 PRO   A CB  1 
ATOM   960  C  CG  . PRO   A 1 124 ? -27.202 4.647   4.114   1.00 49.61  ? 238 PRO   A CG  1 
ATOM   961  C  CD  . PRO   A 1 124 ? -25.891 5.269   3.735   1.00 46.51  ? 238 PRO   A CD  1 
ATOM   962  N  N   . CYS   A 1 125 ? -27.016 2.198   0.438   1.00 40.93  ? 239 CYS   A N   1 
ATOM   963  C  CA  . CYS   A 1 125 ? -27.785 2.047   -0.783  1.00 46.06  ? 239 CYS   A CA  1 
ATOM   964  C  C   . CYS   A 1 125 ? -28.856 1.001   -0.526  1.00 50.62  ? 239 CYS   A C   1 
ATOM   965  O  O   . CYS   A 1 125 ? -28.554 -0.082  -0.017  1.00 50.28  ? 239 CYS   A O   1 
ATOM   966  C  CB  . CYS   A 1 125 ? -26.891 1.619   -1.942  1.00 43.64  ? 239 CYS   A CB  1 
ATOM   967  S  SG  . CYS   A 1 125 ? -27.740 1.527   -3.514  1.00 51.28  ? 239 CYS   A SG  1 
ATOM   968  N  N   . LYS   A 1 126 ? -30.099 1.319   -0.878  1.00 49.47  ? 240 LYS   A N   1 
ATOM   969  C  CA  . LYS   A 1 126 ? -31.212 0.443   -0.544  1.00 53.44  ? 240 LYS   A CA  1 
ATOM   970  C  C   . LYS   A 1 126 ? -31.640 -0.458  -1.696  1.00 50.87  ? 240 LYS   A C   1 
ATOM   971  O  O   . LYS   A 1 126 ? -32.275 -1.489  -1.451  1.00 53.38  ? 240 LYS   A O   1 
ATOM   972  C  CB  . LYS   A 1 126 ? -32.405 1.284   -0.071  1.00 49.69  ? 240 LYS   A CB  1 
ATOM   973  C  CG  . LYS   A 1 126 ? -32.016 2.416   0.891   1.00 57.39  ? 240 LYS   A CG  1 
ATOM   974  C  CD  . LYS   A 1 126 ? -32.217 2.054   2.363   1.00 60.58  ? 240 LYS   A CD  1 
ATOM   975  C  CE  . LYS   A 1 126 ? -32.277 3.324   3.218   1.00 68.90  ? 240 LYS   A CE  1 
ATOM   976  N  NZ  . LYS   A 1 126 ? -31.708 3.165   4.590   1.00 60.89  ? 240 LYS   A NZ  1 
ATOM   977  N  N   . ASN   A 1 127 ? -31.294 -0.110  -2.934  1.00 49.69  ? 241 ASN   A N   1 
ATOM   978  C  CA  . ASN   A 1 127 ? -31.659 -0.878  -4.124  1.00 48.45  ? 241 ASN   A CA  1 
ATOM   979  C  C   . ASN   A 1 127 ? -30.375 -1.432  -4.733  1.00 50.22  ? 241 ASN   A C   1 
ATOM   980  O  O   . ASN   A 1 127 ? -29.817 -0.874  -5.678  1.00 44.14  ? 241 ASN   A O   1 
ATOM   981  C  CB  . ASN   A 1 127 ? -32.423 0.002   -5.121  1.00 50.88  ? 241 ASN   A CB  1 
ATOM   982  C  CG  . ASN   A 1 127 ? -32.951 -0.772  -6.314  1.00 55.65  ? 241 ASN   A CG  1 
ATOM   983  O  OD1 . ASN   A 1 127 ? -32.777 -1.986  -6.421  1.00 53.30  ? 241 ASN   A OD1 1 
ATOM   984  N  ND2 . ASN   A 1 127 ? -33.602 -0.059  -7.226  1.00 61.06  ? 241 ASN   A ND2 1 
ATOM   985  N  N   . VAL   A 1 128 ? -29.909 -2.546  -4.184  1.00 44.87  ? 242 VAL   A N   1 
ATOM   986  C  CA  . VAL   A 1 128 ? -28.634 -3.133  -4.574  1.00 44.42  ? 242 VAL   A CA  1 
ATOM   987  C  C   . VAL   A 1 128 ? -28.881 -4.329  -5.478  1.00 48.35  ? 242 VAL   A C   1 
ATOM   988  O  O   . VAL   A 1 128 ? -29.761 -5.157  -5.214  1.00 47.27  ? 242 VAL   A O   1 
ATOM   989  C  CB  . VAL   A 1 128 ? -27.805 -3.536  -3.338  1.00 46.22  ? 242 VAL   A CB  1 
ATOM   990  C  CG1 . VAL   A 1 128 ? -26.436 -4.054  -3.760  1.00 47.43  ? 242 VAL   A CG1 1 
ATOM   991  C  CG2 . VAL   A 1 128 ? -27.658 -2.358  -2.397  1.00 47.20  ? 242 VAL   A CG2 1 
ATOM   992  N  N   . SER   A 1 129 ? -28.100 -4.412  -6.550  1.00 45.96  ? 243 SER   A N   1 
ATOM   993  C  CA  . SER   A 1 129 ? -28.041 -5.576  -7.413  1.00 45.64  ? 243 SER   A CA  1 
ATOM   994  C  C   . SER   A 1 129 ? -26.596 -6.057  -7.483  1.00 48.47  ? 243 SER   A C   1 
ATOM   995  O  O   . SER   A 1 129 ? -25.663 -5.342  -7.111  1.00 46.96  ? 243 SER   A O   1 
ATOM   996  C  CB  . SER   A 1 129 ? -28.570 -5.262  -8.821  1.00 50.24  ? 243 SER   A CB  1 
ATOM   997  O  OG  . SER   A 1 129 ? -27.671 -4.420  -9.522  1.00 50.08  ? 243 SER   A OG  1 
ATOM   998  N  N   . SER   A 1 130 ? -26.418 -7.282  -7.965  1.00 46.56  ? 244 SER   A N   1 
ATOM   999  C  CA  . SER   A 1 130 ? -25.100 -7.859  -8.173  1.00 46.27  ? 244 SER   A CA  1 
ATOM   1000 C  C   . SER   A 1 130 ? -24.857 -8.008  -9.667  1.00 45.47  ? 244 SER   A C   1 
ATOM   1001 O  O   . SER   A 1 130 ? -25.758 -8.400  -10.414 1.00 49.41  ? 244 SER   A O   1 
ATOM   1002 C  CB  . SER   A 1 130 ? -24.968 -9.216  -7.473  1.00 49.94  ? 244 SER   A CB  1 
ATOM   1003 O  OG  . SER   A 1 130 ? -24.946 -10.279 -8.411  1.00 50.99  ? 244 SER   A OG  1 
ATOM   1004 N  N   . VAL   A 1 131 ? -23.640 -7.683  -10.105 1.00 42.61  ? 245 VAL   A N   1 
ATOM   1005 C  CA  . VAL   A 1 131 ? -23.275 -7.758  -11.513 1.00 40.77  ? 245 VAL   A CA  1 
ATOM   1006 C  C   . VAL   A 1 131 ? -21.909 -8.416  -11.631 1.00 42.24  ? 245 VAL   A C   1 
ATOM   1007 O  O   . VAL   A 1 131 ? -21.106 -8.412  -10.696 1.00 38.52  ? 245 VAL   A O   1 
ATOM   1008 C  CB  . VAL   A 1 131 ? -23.254 -6.368  -12.196 1.00 43.86  ? 245 VAL   A CB  1 
ATOM   1009 C  CG1 . VAL   A 1 131 ? -24.618 -5.713  -12.119 1.00 43.82  ? 245 VAL   A CG1 1 
ATOM   1010 C  CG2 . VAL   A 1 131 ? -22.195 -5.474  -11.575 1.00 36.84  ? 245 VAL   A CG2 1 
ATOM   1011 N  N   . GLN   A 1 132 ? -21.655 -8.989  -12.807 1.00 41.55  ? 246 GLN   A N   1 
ATOM   1012 C  CA  . GLN   A 1 132 ? -20.339 -9.524  -13.126 1.00 43.94  ? 246 GLN   A CA  1 
ATOM   1013 C  C   . GLN   A 1 132 ? -19.383 -8.440  -13.599 1.00 42.59  ? 246 GLN   A C   1 
ATOM   1014 O  O   . GLN   A 1 132 ? -18.184 -8.494  -13.297 1.00 38.31  ? 246 GLN   A O   1 
ATOM   1015 C  CB  . GLN   A 1 132 ? -20.455 -10.596 -14.209 1.00 40.97  ? 246 GLN   A CB  1 
ATOM   1016 C  CG  . GLN   A 1 132 ? -20.784 -11.972 -13.687 1.00 48.95  ? 246 GLN   A CG  1 
ATOM   1017 C  CD  . GLN   A 1 132 ? -21.915 -12.609 -14.466 1.00 56.80  ? 246 GLN   A CD  1 
ATOM   1018 O  OE1 . GLN   A 1 132 ? -22.658 -11.928 -15.176 1.00 56.53  ? 246 GLN   A OE1 1 
ATOM   1019 N  NE2 . GLN   A 1 132 ? -22.050 -13.925 -14.343 1.00 52.52  ? 246 GLN   A NE2 1 
ATOM   1020 N  N   . CYS   A 1 133 ? -19.901 -7.449  -14.317 1.00 39.62  ? 247 CYS   A N   1 
ATOM   1021 C  CA  . CYS   A 1 133 ? -19.100 -6.374  -14.874 1.00 38.14  ? 247 CYS   A CA  1 
ATOM   1022 C  C   . CYS   A 1 133 ? -19.823 -5.054  -14.692 1.00 36.63  ? 247 CYS   A C   1 
ATOM   1023 O  O   . CYS   A 1 133 ? -21.053 -5.006  -14.605 1.00 35.97  ? 247 CYS   A O   1 
ATOM   1024 C  CB  . CYS   A 1 133 ? -18.820 -6.586  -16.364 1.00 38.19  ? 247 CYS   A CB  1 
ATOM   1025 S  SG  . CYS   A 1 133 ? -17.927 -8.086  -16.757 1.00 41.61  ? 247 CYS   A SG  1 
ATOM   1026 N  N   . THR   A 1 134 ? -19.044 -3.978  -14.643 1.00 36.32  ? 248 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 134 ? -19.620 -2.648  -14.725 1.00 34.28  ? 248 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 134 ? -20.170 -2.419  -16.129 1.00 33.23  ? 248 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 134 ? -19.972 -3.223  -17.044 1.00 31.43  ? 248 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 134 ? -18.578 -1.587  -14.387 1.00 29.60  ? 248 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 134 ? -17.531 -1.622  -15.364 1.00 32.23  ? 248 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 134 ? -17.992 -1.840  -13.022 1.00 32.09  ? 248 THR   A CG2 1 
ATOM   1033 N  N   . HIS   A 1 135 ? -20.879 -1.310  -16.301 1.00 29.49  ? 249 HIS   A N   1 
ATOM   1034 C  CA  . HIS   A 1 135 ? -21.202 -0.875  -17.646 1.00 34.14  ? 249 HIS   A CA  1 
ATOM   1035 C  C   . HIS   A 1 135 ? -19.944 -0.328  -18.312 1.00 35.54  ? 249 HIS   A C   1 
ATOM   1036 O  O   . HIS   A 1 135 ? -18.898 -0.153  -17.680 1.00 33.78  ? 249 HIS   A O   1 
ATOM   1037 C  CB  . HIS   A 1 135 ? -22.276 0.207   -17.630 1.00 27.93  ? 249 HIS   A CB  1 
ATOM   1038 C  CG  . HIS   A 1 135 ? -21.808 1.494   -17.031 1.00 31.05  ? 249 HIS   A CG  1 
ATOM   1039 N  ND1 . HIS   A 1 135 ? -21.616 1.661   -15.678 1.00 30.37  ? 249 HIS   A ND1 1 
ATOM   1040 C  CD2 . HIS   A 1 135 ? -21.483 2.677   -17.604 1.00 36.25  ? 249 HIS   A CD2 1 
ATOM   1041 C  CE1 . HIS   A 1 135 ? -21.191 2.890   -15.443 1.00 36.03  ? 249 HIS   A CE1 1 
ATOM   1042 N  NE2 . HIS   A 1 135 ? -21.105 3.528   -16.595 1.00 35.13  ? 249 HIS   A NE2 1 
ATOM   1043 N  N   . GLY   A 1 136 ? -20.057 -0.037  -19.604 1.00 30.09  ? 250 GLY   A N   1 
ATOM   1044 C  CA  . GLY   A 1 136 ? -18.937 0.508   -20.343 1.00 33.53  ? 250 GLY   A CA  1 
ATOM   1045 C  C   . GLY   A 1 136 ? -18.637 1.942   -19.963 1.00 32.87  ? 250 GLY   A C   1 
ATOM   1046 O  O   . GLY   A 1 136 ? -19.447 2.840   -20.212 1.00 34.46  ? 250 GLY   A O   1 
ATOM   1047 N  N   . ILE   A 1 137 ? -17.484 2.170   -19.341 1.00 28.45  ? 251 ILE   A N   1 
ATOM   1048 C  CA  . ILE   A 1 137 ? -17.070 3.501   -18.915 1.00 28.22  ? 251 ILE   A CA  1 
ATOM   1049 C  C   . ILE   A 1 137 ? -16.008 4.014   -19.876 1.00 30.44  ? 251 ILE   A C   1 
ATOM   1050 O  O   . ILE   A 1 137 ? -14.984 3.352   -20.096 1.00 30.36  ? 251 ILE   A O   1 
ATOM   1051 C  CB  . ILE   A 1 137 ? -16.541 3.486   -17.472 1.00 29.83  ? 251 ILE   A CB  1 
ATOM   1052 C  CG1 . ILE   A 1 137 ? -17.684 3.240   -16.488 1.00 30.72  ? 251 ILE   A CG1 1 
ATOM   1053 C  CG2 . ILE   A 1 137 ? -15.892 4.817   -17.147 1.00 33.78  ? 251 ILE   A CG2 1 
ATOM   1054 C  CD1 . ILE   A 1 137 ? -17.222 2.781   -15.123 1.00 31.93  ? 251 ILE   A CD1 1 
ATOM   1055 N  N   . LYS   A 1 138 ? -16.256 5.193   -20.448 1.00 28.53  ? 252 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 138 ? -15.260 5.877   -21.266 1.00 26.84  ? 252 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 138 ? -14.221 6.535   -20.366 1.00 26.71  ? 252 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 138 ? -14.584 7.320   -19.482 1.00 26.67  ? 252 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 138 ? -15.912 6.934   -22.144 1.00 30.82  ? 252 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 138 ? -16.534 6.411   -23.423 1.00 31.77  ? 252 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 138 ? -17.154 7.572   -24.200 1.00 33.52  ? 252 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 138 ? -17.886 7.103   -25.454 1.00 36.14  ? 252 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 138 ? -17.899 8.178   -26.498 1.00 40.67  ? 252 LYS   A NZ  1 
ATOM   1064 N  N   . PRO   A 1 139 ? -12.936 6.253   -20.558 1.00 27.73  ? 253 PRO   A N   1 
ATOM   1065 C  CA  . PRO   A 1 139 ? -11.896 6.892   -19.726 1.00 25.46  ? 253 PRO   A CA  1 
ATOM   1066 C  C   . PRO   A 1 139 ? -11.503 8.278   -20.221 1.00 25.45  ? 253 PRO   A C   1 
ATOM   1067 O  O   . PRO   A 1 139 ? -10.414 8.507   -20.766 1.00 28.71  ? 253 PRO   A O   1 
ATOM   1068 C  CB  . PRO   A 1 139 ? -10.744 5.896   -19.834 1.00 24.65  ? 253 PRO   A CB  1 
ATOM   1069 C  CG  . PRO   A 1 139 ? -10.892 5.317   -21.190 1.00 27.39  ? 253 PRO   A CG  1 
ATOM   1070 C  CD  . PRO   A 1 139 ? -12.379 5.196   -21.419 1.00 29.20  ? 253 PRO   A CD  1 
ATOM   1071 N  N   . VAL   A 1 140 ? -12.394 9.245   -20.029 1.00 27.31  ? 254 VAL   A N   1 
ATOM   1072 C  CA  . VAL   A 1 140 ? -12.200 10.582  -20.572 1.00 28.15  ? 254 VAL   A CA  1 
ATOM   1073 C  C   . VAL   A 1 140 ? -11.379 11.399  -19.588 1.00 26.49  ? 254 VAL   A C   1 
ATOM   1074 O  O   . VAL   A 1 140 ? -11.826 11.679  -18.472 1.00 26.68  ? 254 VAL   A O   1 
ATOM   1075 C  CB  . VAL   A 1 140 ? -13.544 11.257  -20.873 1.00 27.26  ? 254 VAL   A CB  1 
ATOM   1076 C  CG1 . VAL   A 1 140 ? -13.314 12.655  -21.410 1.00 27.62  ? 254 VAL   A CG1 1 
ATOM   1077 C  CG2 . VAL   A 1 140 ? -14.339 10.413  -21.855 1.00 23.82  ? 254 VAL   A CG2 1 
ATOM   1078 N  N   . VAL   A 1 141 ? -10.176 11.767  -20.000 1.00 24.40  ? 255 VAL   A N   1 
ATOM   1079 C  CA  . VAL   A 1 141 ? -9.293  12.582  -19.175 1.00 24.27  ? 255 VAL   A CA  1 
ATOM   1080 C  C   . VAL   A 1 141 ? -9.638  14.052  -19.368 1.00 25.29  ? 255 VAL   A C   1 
ATOM   1081 O  O   . VAL   A 1 141 ? -9.706  14.539  -20.502 1.00 22.86  ? 255 VAL   A O   1 
ATOM   1082 C  CB  . VAL   A 1 141 ? -7.825  12.301  -19.525 1.00 23.60  ? 255 VAL   A CB  1 
ATOM   1083 C  CG1 . VAL   A 1 141 ? -6.909  13.216  -18.737 1.00 25.72  ? 255 VAL   A CG1 1 
ATOM   1084 C  CG2 . VAL   A 1 141 ? -7.496  10.851  -19.222 1.00 23.38  ? 255 VAL   A CG2 1 
ATOM   1085 N  N   . SER   A 1 142 ? -9.866  14.763  -18.265 1.00 24.09  ? 256 SER   A N   1 
ATOM   1086 C  CA  . SER   A 1 142 ? -10.182 16.185  -18.345 1.00 23.93  ? 256 SER   A CA  1 
ATOM   1087 C  C   . SER   A 1 142 ? -10.034 16.820  -16.969 1.00 26.99  ? 256 SER   A C   1 
ATOM   1088 O  O   . SER   A 1 142 ? -9.924  16.136  -15.948 1.00 24.74  ? 256 SER   A O   1 
ATOM   1089 C  CB  . SER   A 1 142 ? -11.599 16.424  -18.879 1.00 27.04  ? 256 SER   A CB  1 
ATOM   1090 O  OG  . SER   A 1 142 ? -12.567 15.946  -17.960 1.00 28.21  ? 256 SER   A OG  1 
ATOM   1091 N  N   . THR   A 1 143 ? -10.051 18.148  -16.958 1.00 22.11  ? 257 THR   A N   1 
ATOM   1092 C  CA  . THR   A 1 143 ? -10.136 18.935  -15.742 1.00 27.08  ? 257 THR   A CA  1 
ATOM   1093 C  C   . THR   A 1 143 ? -11.348 19.852  -15.820 1.00 23.54  ? 257 THR   A C   1 
ATOM   1094 O  O   . THR   A 1 143 ? -11.857 20.143  -16.905 1.00 24.69  ? 257 THR   A O   1 
ATOM   1095 C  CB  . THR   A 1 143 ? -8.860  19.758  -15.525 1.00 26.93  ? 257 THR   A CB  1 
ATOM   1096 O  OG1 . THR   A 1 143 ? -8.772  20.783  -16.524 1.00 26.85  ? 257 THR   A OG1 1 
ATOM   1097 C  CG2 . THR   A 1 143 ? -7.642  18.866  -15.594 1.00 25.63  ? 257 THR   A CG2 1 
ATOM   1098 N  N   . GLN   A 1 144 ? -11.802 20.303  -14.646 1.00 22.44  ? 258 GLN   A N   1 
ATOM   1099 C  CA  . GLN   A 1 144 ? -12.945 21.203  -14.490 1.00 23.44  ? 258 GLN   A CA  1 
ATOM   1100 C  C   . GLN   A 1 144 ? -14.261 20.601  -14.956 1.00 23.77  ? 258 GLN   A C   1 
ATOM   1101 O  O   . GLN   A 1 144 ? -15.221 20.538  -14.182 1.00 27.02  ? 258 GLN   A O   1 
ATOM   1102 C  CB  . GLN   A 1 144 ? -12.716 22.539  -15.208 1.00 25.28  ? 258 GLN   A CB  1 
ATOM   1103 C  CG  . GLN   A 1 144 ? -11.343 23.148  -15.031 1.00 26.35  ? 258 GLN   A CG  1 
ATOM   1104 C  CD  . GLN   A 1 144 ? -11.343 24.635  -15.340 1.00 32.43  ? 258 GLN   A CD  1 
ATOM   1105 O  OE1 . GLN   A 1 144 ? -12.288 25.155  -15.935 1.00 24.07  ? 258 GLN   A OE1 1 
ATOM   1106 N  NE2 . GLN   A 1 144 ? -10.293 25.333  -14.910 1.00 30.15  ? 258 GLN   A NE2 1 
ATOM   1107 N  N   . LEU   A 1 145 ? -14.330 20.171  -16.209 1.00 21.40  ? 259 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 145 ? -15.562 19.660  -16.789 1.00 26.12  ? 259 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 145 ? -15.410 18.174  -17.076 1.00 26.33  ? 259 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 145 ? -14.446 17.758  -17.728 1.00 29.60  ? 259 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 145 ? -15.919 20.423  -18.067 1.00 23.31  ? 259 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 145 ? -16.027 21.945  -17.959 1.00 27.42  ? 259 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 145 ? -16.271 22.563  -19.329 1.00 31.01  ? 259 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 145 ? -17.125 22.340  -16.987 1.00 31.13  ? 259 LEU   A CD2 1 
ATOM   1115 N  N   . LEU   A 1 146 ? -16.353 17.378  -16.579 1.00 27.35  ? 260 LEU   A N   1 
ATOM   1116 C  CA  . LEU   A 1 146 ? -16.373 15.951  -16.852 1.00 24.65  ? 260 LEU   A CA  1 
ATOM   1117 C  C   . LEU   A 1 146 ? -17.129 15.731  -18.153 1.00 29.31  ? 260 LEU   A C   1 
ATOM   1118 O  O   . LEU   A 1 146 ? -18.265 16.193  -18.302 1.00 29.67  ? 260 LEU   A O   1 
ATOM   1119 C  CB  . LEU   A 1 146 ? -17.026 15.181  -15.703 1.00 23.93  ? 260 LEU   A CB  1 
ATOM   1120 C  CG  . LEU   A 1 146 ? -16.190 15.166  -14.415 1.00 29.22  ? 260 LEU   A CG  1 
ATOM   1121 C  CD1 . LEU   A 1 146 ? -16.944 14.492  -13.280 1.00 32.29  ? 260 LEU   A CD1 1 
ATOM   1122 C  CD2 . LEU   A 1 146 ? -14.822 14.521  -14.628 1.00 33.47  ? 260 LEU   A CD2 1 
ATOM   1123 N  N   . LEU   A 1 147 ? -16.487 15.054  -19.099 1.00 27.02  ? 261 LEU   A N   1 
ATOM   1124 C  CA  . LEU   A 1 147 ? -16.985 14.956  -20.460 1.00 27.29  ? 261 LEU   A CA  1 
ATOM   1125 C  C   . LEU   A 1 147 ? -17.405 13.536  -20.804 1.00 30.22  ? 261 LEU   A C   1 
ATOM   1126 O  O   . LEU   A 1 147 ? -16.765 12.563  -20.388 1.00 27.31  ? 261 LEU   A O   1 
ATOM   1127 C  CB  . LEU   A 1 147 ? -15.929 15.427  -21.467 1.00 26.79  ? 261 LEU   A CB  1 
ATOM   1128 C  CG  . LEU   A 1 147 ? -15.379 16.834  -21.261 1.00 24.53  ? 261 LEU   A CG  1 
ATOM   1129 C  CD1 . LEU   A 1 147 ? -14.214 17.098  -22.217 1.00 26.67  ? 261 LEU   A CD1 1 
ATOM   1130 C  CD2 . LEU   A 1 147 ? -16.480 17.869  -21.447 1.00 29.31  ? 261 LEU   A CD2 1 
ATOM   1131 N  N   . ASN   A 1 148 ? -18.482 13.436  -21.585 1.00 29.51  ? 262 ASN   A N   1 
ATOM   1132 C  CA  . ASN   A 1 148 ? -18.919 12.180  -22.194 1.00 29.14  ? 262 ASN   A CA  1 
ATOM   1133 C  C   . ASN   A 1 148 ? -19.248 11.108  -21.161 1.00 34.32  ? 262 ASN   A C   1 
ATOM   1134 O  O   . ASN   A 1 148 ? -19.196 9.912   -21.451 1.00 28.61  ? 262 ASN   A O   1 
ATOM   1135 C  CB  . ASN   A 1 148 ? -17.877 11.657  -23.182 1.00 29.34  ? 262 ASN   A CB  1 
ATOM   1136 C  CG  . ASN   A 1 148 ? -17.913 12.388  -24.497 1.00 31.25  ? 262 ASN   A CG  1 
ATOM   1137 O  OD1 . ASN   A 1 148 ? -18.806 13.201  -24.748 1.00 32.94  ? 262 ASN   A OD1 1 
ATOM   1138 N  ND2 . ASN   A 1 148 ? -16.957 12.089  -25.359 1.00 31.31  ? 262 ASN   A ND2 1 
ATOM   1139 N  N   . GLY   A 1 149 ? -19.594 11.513  -19.953 1.00 29.02  ? 263 GLY   A N   1 
ATOM   1140 C  CA  . GLY   A 1 149 ? -19.926 10.584  -18.898 1.00 33.22  ? 263 GLY   A CA  1 
ATOM   1141 C  C   . GLY   A 1 149 ? -21.393 10.215  -18.912 1.00 33.05  ? 263 GLY   A C   1 
ATOM   1142 O  O   . GLY   A 1 149 ? -22.134 10.499  -19.859 1.00 33.57  ? 263 GLY   A O   1 
ATOM   1143 N  N   . SER   A 1 150 ? -21.812 9.564   -17.837 1.00 31.35  ? 264 SER   A N   1 
ATOM   1144 C  CA  . SER   A 1 150 ? -23.222 9.349   -17.575 1.00 35.24  ? 264 SER   A CA  1 
ATOM   1145 C  C   . SER   A 1 150 ? -23.798 10.587  -16.900 1.00 36.33  ? 264 SER   A C   1 
ATOM   1146 O  O   . SER   A 1 150 ? -23.072 11.450  -16.399 1.00 36.65  ? 264 SER   A O   1 
ATOM   1147 C  CB  . SER   A 1 150 ? -23.440 8.118   -16.692 1.00 32.28  ? 264 SER   A CB  1 
ATOM   1148 O  OG  . SER   A 1 150 ? -22.930 8.329   -15.385 1.00 35.76  ? 264 SER   A OG  1 
ATOM   1149 N  N   . LEU   A 1 151 ? -25.120 10.668  -16.896 1.00 34.58  ? 265 LEU   A N   1 
ATOM   1150 C  CA  . LEU   A 1 151 ? -25.836 11.754  -16.253 1.00 37.19  ? 265 LEU   A CA  1 
ATOM   1151 C  C   . LEU   A 1 151 ? -26.524 11.220  -15.007 1.00 35.86  ? 265 LEU   A C   1 
ATOM   1152 O  O   . LEU   A 1 151 ? -26.852 10.035  -14.916 1.00 36.30  ? 265 LEU   A O   1 
ATOM   1153 C  CB  . LEU   A 1 151 ? -26.859 12.370  -17.216 1.00 37.07  ? 265 LEU   A CB  1 
ATOM   1154 C  CG  . LEU   A 1 151 ? -26.250 13.166  -18.376 1.00 38.24  ? 265 LEU   A CG  1 
ATOM   1155 C  CD1 . LEU   A 1 151 ? -27.306 13.526  -19.422 1.00 34.45  ? 265 LEU   A CD1 1 
ATOM   1156 C  CD2 . LEU   A 1 151 ? -25.542 14.419  -17.873 1.00 36.24  ? 265 LEU   A CD2 1 
ATOM   1157 N  N   . ALA   A 1 152 ? -26.716 12.106  -14.035 1.00 35.53  ? 266 ALA   A N   1 
ATOM   1158 C  CA  . ALA   A 1 152 ? -27.478 11.755  -12.847 1.00 38.17  ? 266 ALA   A CA  1 
ATOM   1159 C  C   . ALA   A 1 152 ? -28.923 11.495  -13.246 1.00 40.21  ? 266 ALA   A C   1 
ATOM   1160 O  O   . ALA   A 1 152 ? -29.469 12.174  -14.121 1.00 37.23  ? 266 ALA   A O   1 
ATOM   1161 C  CB  . ALA   A 1 152 ? -27.394 12.865  -11.802 1.00 37.97  ? 266 ALA   A CB  1 
ATOM   1162 N  N   . GLU   A 1 153 ? -29.540 10.489  -12.621 1.00 47.76  ? 267 GLU   A N   1 
ATOM   1163 C  CA  . GLU   A 1 153 ? -30.833 10.020  -13.111 1.00 49.81  ? 267 GLU   A CA  1 
ATOM   1164 C  C   . GLU   A 1 153 ? -31.968 10.976  -12.748 1.00 43.82  ? 267 GLU   A C   1 
ATOM   1165 O  O   . GLU   A 1 153 ? -32.863 11.218  -13.566 1.00 46.24  ? 267 GLU   A O   1 
ATOM   1166 C  CB  . GLU   A 1 153 ? -31.099 8.602   -12.604 1.00 50.87  ? 267 GLU   A CB  1 
ATOM   1167 C  CG  . GLU   A 1 153 ? -30.360 7.530   -13.413 1.00 54.29  ? 267 GLU   A CG  1 
ATOM   1168 C  CD  . GLU   A 1 153 ? -29.960 6.320   -12.588 1.00 60.68  ? 267 GLU   A CD  1 
ATOM   1169 O  OE1 . GLU   A 1 153 ? -29.084 6.452   -11.703 1.00 62.73  ? 267 GLU   A OE1 1 
ATOM   1170 O  OE2 . GLU   A 1 153 ? -30.530 5.231   -12.819 1.00 60.90  ? 267 GLU   A OE2 1 
ATOM   1171 N  N   . GLU   A 1 154 ? -31.947 11.557  -11.546 1.00 46.90  ? 268 GLU   A N   1 
ATOM   1172 C  CA  . GLU   A 1 154 ? -33.025 12.438  -11.123 1.00 45.62  ? 268 GLU   A CA  1 
ATOM   1173 C  C   . GLU   A 1 154 ? -32.484 13.856  -11.016 1.00 46.12  ? 268 GLU   A C   1 
ATOM   1174 O  O   . GLU   A 1 154 ? -32.434 14.581  -12.027 1.00 44.82  ? 268 GLU   A O   1 
ATOM   1175 C  CB  . GLU   A 1 154 ? -33.638 11.960  -9.803  1.00 52.62  ? 268 GLU   A CB  1 
ATOM   1176 C  CG  . GLU   A 1 154 ? -34.290 10.600  -9.828  1.00 53.31  ? 268 GLU   A CG  1 
ATOM   1177 C  CD  . GLU   A 1 154 ? -34.875 10.248  -8.470  1.00 61.12  ? 268 GLU   A CD  1 
ATOM   1178 O  OE1 . GLU   A 1 154 ? -34.657 11.029  -7.516  1.00 71.06  ? 268 GLU   A OE1 1 
ATOM   1179 O  OE2 . GLU   A 1 154 ? -35.549 9.201   -8.346  1.00 67.86  ? 268 GLU   A OE2 1 
ATOM   1180 N  N   . GLU   A 1 155 ? -32.096 14.307  -9.830  1.00 44.63  ? 269 GLU   A N   1 
ATOM   1181 C  CA  . GLU   A 1 155 ? -31.638 15.665  -9.613  1.00 46.09  ? 269 GLU   A CA  1 
ATOM   1182 C  C   . GLU   A 1 155 ? -30.138 15.750  -9.863  1.00 46.11  ? 269 GLU   A C   1 
ATOM   1183 O  O   . GLU   A 1 155 ? -29.448 14.741  -10.030 1.00 41.15  ? 269 GLU   A O   1 
ATOM   1184 C  CB  . GLU   A 1 155 ? -31.972 16.095  -8.184  1.00 47.69  ? 269 GLU   A CB  1 
ATOM   1185 C  CG  . GLU   A 1 155 ? -33.395 15.752  -7.780  1.00 48.95  ? 269 GLU   A CG  1 
ATOM   1186 C  CD  . GLU   A 1 155 ? -34.084 16.857  -7.008  1.00 54.42  ? 269 GLU   A CD  1 
ATOM   1187 O  OE1 . GLU   A 1 155 ? -33.459 17.917  -6.784  1.00 51.14  ? 269 GLU   A OE1 1 
ATOM   1188 O  OE2 . GLU   A 1 155 ? -35.258 16.662  -6.621  1.00 54.75  ? 269 GLU   A OE2 1 
ATOM   1189 N  N   . ILE   A 1 156 ? -29.631 16.981  -9.894  1.00 42.23  ? 270 ILE   A N   1 
ATOM   1190 C  CA  . ILE   A 1 156 ? -28.189 17.180  -9.871  1.00 41.85  ? 270 ILE   A CA  1 
ATOM   1191 C  C   . ILE   A 1 156 ? -27.662 16.667  -8.540  1.00 40.45  ? 270 ILE   A C   1 
ATOM   1192 O  O   . ILE   A 1 156 ? -28.181 17.020  -7.475  1.00 41.62  ? 270 ILE   A O   1 
ATOM   1193 C  CB  . ILE   A 1 156 ? -27.840 18.661  -10.083 1.00 38.42  ? 270 ILE   A CB  1 
ATOM   1194 C  CG1 . ILE   A 1 156 ? -28.240 19.104  -11.489 1.00 34.23  ? 270 ILE   A CG1 1 
ATOM   1195 C  CG2 . ILE   A 1 156 ? -26.359 18.896  -9.887  1.00 34.59  ? 270 ILE   A CG2 1 
ATOM   1196 C  CD1 . ILE   A 1 156 ? -28.039 20.568  -11.749 1.00 41.18  ? 270 ILE   A CD1 1 
ATOM   1197 N  N   . ILE   A 1 157 ? -26.647 15.811  -8.589  1.00 38.16  ? 271 ILE   A N   1 
ATOM   1198 C  CA  . ILE   A 1 157 ? -26.099 15.177  -7.395  1.00 39.64  ? 271 ILE   A CA  1 
ATOM   1199 C  C   . ILE   A 1 157 ? -24.778 15.844  -7.039  1.00 34.98  ? 271 ILE   A C   1 
ATOM   1200 O  O   . ILE   A 1 157 ? -23.919 16.046  -7.906  1.00 35.94  ? 271 ILE   A O   1 
ATOM   1201 C  CB  . ILE   A 1 157 ? -25.918 13.661  -7.587  1.00 36.95  ? 271 ILE   A CB  1 
ATOM   1202 C  CG1 . ILE   A 1 157 ? -27.176 13.042  -8.195  1.00 39.87  ? 271 ILE   A CG1 1 
ATOM   1203 C  CG2 . ILE   A 1 157 ? -25.584 12.993  -6.268  1.00 40.26  ? 271 ILE   A CG2 1 
ATOM   1204 C  CD1 . ILE   A 1 157 ? -28.358 13.027  -7.257  1.00 42.75  ? 271 ILE   A CD1 1 
ATOM   1205 N  N   . ILE   A 1 158 ? -24.621 16.177  -5.761  1.00 35.60  ? 272 ILE   A N   1 
ATOM   1206 C  CA  . ILE   A 1 158 ? -23.369 16.679  -5.213  1.00 37.15  ? 272 ILE   A CA  1 
ATOM   1207 C  C   . ILE   A 1 158 ? -22.651 15.503  -4.568  1.00 38.24  ? 272 ILE   A C   1 
ATOM   1208 O  O   . ILE   A 1 158 ? -23.220 14.816  -3.710  1.00 41.47  ? 272 ILE   A O   1 
ATOM   1209 C  CB  . ILE   A 1 158 ? -23.617 17.798  -4.187  1.00 41.96  ? 272 ILE   A CB  1 
ATOM   1210 C  CG1 . ILE   A 1 158 ? -24.408 18.953  -4.809  1.00 40.64  ? 272 ILE   A CG1 1 
ATOM   1211 C  CG2 . ILE   A 1 158 ? -22.298 18.306  -3.638  1.00 42.08  ? 272 ILE   A CG2 1 
ATOM   1212 C  CD1 . ILE   A 1 158 ? -23.764 19.544  -6.052  1.00 38.36  ? 272 ILE   A CD1 1 
ATOM   1213 N  N   . ARG   A 1 159 ? -21.415 15.255  -4.986  1.00 33.85  ? 273 ARG   A N   1 
ATOM   1214 C  CA  . ARG   A 1 159 ? -20.604 14.183  -4.427  1.00 38.53  ? 273 ARG   A CA  1 
ATOM   1215 C  C   . ARG   A 1 159 ? -19.347 14.767  -3.803  1.00 35.11  ? 273 ARG   A C   1 
ATOM   1216 O  O   . ARG   A 1 159 ? -18.657 15.579  -4.428  1.00 37.25  ? 273 ARG   A O   1 
ATOM   1217 C  CB  . ARG   A 1 159 ? -20.244 13.144  -5.493  1.00 30.61  ? 273 ARG   A CB  1 
ATOM   1218 C  CG  . ARG   A 1 159 ? -21.400 12.769  -6.414  1.00 33.76  ? 273 ARG   A CG  1 
ATOM   1219 C  CD  . ARG   A 1 159 ? -21.017 11.624  -7.338  1.00 33.08  ? 273 ARG   A CD  1 
ATOM   1220 N  NE  . ARG   A 1 159 ? -22.062 11.327  -8.310  1.00 33.10  ? 273 ARG   A NE  1 
ATOM   1221 C  CZ  . ARG   A 1 159 ? -23.128 10.584  -8.045  1.00 37.25  ? 273 ARG   A CZ  1 
ATOM   1222 N  NH1 . ARG   A 1 159 ? -23.335 10.073  -6.842  1.00 38.40  ? 273 ARG   A NH1 1 
ATOM   1223 N  NH2 . ARG   A 1 159 ? -24.009 10.344  -9.011  1.00 36.68  ? 273 ARG   A NH2 1 
ATOM   1224 N  N   . SER   A 1 160 ? -19.065 14.358  -2.568  1.00 36.37  ? 274 SER   A N   1 
ATOM   1225 C  CA  . SER   A 1 160 ? -17.854 14.752  -1.865  1.00 35.67  ? 274 SER   A CA  1 
ATOM   1226 C  C   . SER   A 1 160 ? -17.645 13.797  -0.698  1.00 38.04  ? 274 SER   A C   1 
ATOM   1227 O  O   . SER   A 1 160 ? -18.615 13.369  -0.067  1.00 38.01  ? 274 SER   A O   1 
ATOM   1228 C  CB  . SER   A 1 160 ? -17.928 16.200  -1.377  1.00 37.34  ? 274 SER   A CB  1 
ATOM   1229 O  OG  . SER   A 1 160 ? -16.880 16.473  -0.462  1.00 41.14  ? 274 SER   A OG  1 
ATOM   1230 N  N   . GLU   A 1 161 ? -16.379 13.461  -0.423  1.00 37.45  ? 275 GLU   A N   1 
ATOM   1231 C  CA  . GLU   A 1 161 ? -16.063 12.645  0.745   1.00 37.99  ? 275 GLU   A CA  1 
ATOM   1232 C  C   . GLU   A 1 161 ? -16.561 13.280  2.032   1.00 42.23  ? 275 GLU   A C   1 
ATOM   1233 O  O   . GLU   A 1 161 ? -16.858 12.567  2.998   1.00 43.28  ? 275 GLU   A O   1 
ATOM   1234 C  CB  . GLU   A 1 161 ? -14.555 12.431  0.840   1.00 40.78  ? 275 GLU   A CB  1 
ATOM   1235 C  CG  . GLU   A 1 161 ? -14.146 11.287  1.733   1.00 38.38  ? 275 GLU   A CG  1 
ATOM   1236 C  CD  . GLU   A 1 161 ? -12.706 10.891  1.509   1.00 43.62  ? 275 GLU   A CD  1 
ATOM   1237 O  OE1 . GLU   A 1 161 ? -11.892 11.780  1.168   1.00 43.91  ? 275 GLU   A OE1 1 
ATOM   1238 O  OE2 . GLU   A 1 161 ? -12.380 9.698   1.682   1.00 45.24  ? 275 GLU   A OE2 1 
ATOM   1239 N  N   . ASN   A 1 162 ? -16.658 14.605  2.058   1.00 41.09  ? 276 ASN   A N   1 
ATOM   1240 C  CA  . ASN   A 1 162 ? -17.047 15.354  3.240   1.00 43.32  ? 276 ASN   A CA  1 
ATOM   1241 C  C   . ASN   A 1 162 ? -17.223 16.809  2.840   1.00 45.69  ? 276 ASN   A C   1 
ATOM   1242 O  O   . ASN   A 1 162 ? -16.255 17.577  2.786   1.00 41.13  ? 276 ASN   A O   1 
ATOM   1243 C  CB  . ASN   A 1 162 ? -16.004 15.193  4.344   1.00 48.56  ? 276 ASN   A CB  1 
ATOM   1244 C  CG  . ASN   A 1 162 ? -16.319 16.009  5.582   1.00 50.86  ? 276 ASN   A CG  1 
ATOM   1245 O  OD1 . ASN   A 1 162 ? -17.389 16.607  5.717   1.00 47.40  ? 276 ASN   A OD1 1 
ATOM   1246 N  ND2 . ASN   A 1 162 ? -15.375 16.029  6.500   1.00 50.66  ? 276 ASN   A ND2 1 
ATOM   1247 N  N   . LEU   A 1 163 ? -18.469 17.176  2.544   1.00 46.05  ? 277 LEU   A N   1 
ATOM   1248 C  CA  . LEU   A 1 163 ? -18.780 18.515  2.064   1.00 43.77  ? 277 LEU   A CA  1 
ATOM   1249 C  C   . LEU   A 1 163 ? -18.239 19.582  3.003   1.00 45.54  ? 277 LEU   A C   1 
ATOM   1250 O  O   . LEU   A 1 163 ? -17.780 20.644  2.561   1.00 38.58  ? 277 LEU   A O   1 
ATOM   1251 C  CB  . LEU   A 1 163 ? -20.292 18.639  1.921   1.00 42.69  ? 277 LEU   A CB  1 
ATOM   1252 C  CG  . LEU   A 1 163 ? -20.840 18.558  0.505   1.00 47.75  ? 277 LEU   A CG  1 
ATOM   1253 C  CD1 . LEU   A 1 163 ? -22.189 19.163  0.520   1.00 42.37  ? 277 LEU   A CD1 1 
ATOM   1254 C  CD2 . LEU   A 1 163 ? -19.938 19.317  -0.454  1.00 39.37  ? 277 LEU   A CD2 1 
ATOM   1255 N  N   . THR   A 1 164 ? -18.279 19.306  4.309   1.00 47.01  ? 278 THR   A N   1 
ATOM   1256 C  CA  . THR   A 1 164 ? -17.823 20.269  5.302   1.00 48.13  ? 278 THR   A CA  1 
ATOM   1257 C  C   . THR   A 1 164 ? -16.330 20.544  5.183   1.00 48.07  ? 278 THR   A C   1 
ATOM   1258 O  O   . THR   A 1 164 ? -15.873 21.635  5.540   1.00 46.03  ? 278 THR   A O   1 
ATOM   1259 C  CB  . THR   A 1 164 ? -18.170 19.759  6.698   1.00 50.62  ? 278 THR   A CB  1 
ATOM   1260 O  OG1 . THR   A 1 164 ? -19.573 19.486  6.756   1.00 57.45  ? 278 THR   A OG1 1 
ATOM   1261 C  CG2 . THR   A 1 164 ? -17.849 20.794  7.759   1.00 48.10  ? 278 THR   A CG2 1 
ATOM   1262 N  N   . ASN   A 1 165 ? -15.559 19.580  4.682   1.00 46.29  ? 279 ASN   A N   1 
ATOM   1263 C  CA  . ASN   A 1 165 ? -14.129 19.764  4.457   1.00 45.99  ? 279 ASN   A CA  1 
ATOM   1264 C  C   . ASN   A 1 165 ? -13.919 20.413  3.096   1.00 42.15  ? 279 ASN   A C   1 
ATOM   1265 O  O   . ASN   A 1 165 ? -14.209 19.802  2.063   1.00 41.65  ? 279 ASN   A O   1 
ATOM   1266 C  CB  . ASN   A 1 165 ? -13.401 18.422  4.531   1.00 46.43  ? 279 ASN   A CB  1 
ATOM   1267 C  CG  . ASN   A 1 165 ? -11.883 18.570  4.578   1.00 40.56  ? 279 ASN   A CG  1 
ATOM   1268 O  OD1 . ASN   A 1 165 ? -11.332 19.624  4.247   1.00 43.84  ? 279 ASN   A OD1 1 
ATOM   1269 N  ND2 . ASN   A 1 165 ? -11.200 17.506  4.996   1.00 43.13  ? 279 ASN   A ND2 1 
ATOM   1270 N  N   . ASN   A 1 166 ? -13.409 21.648  3.094   1.00 38.56  ? 280 ASN   A N   1 
ATOM   1271 C  CA  . ASN   A 1 166 ? -13.240 22.380  1.844   1.00 42.07  ? 280 ASN   A CA  1 
ATOM   1272 C  C   . ASN   A 1 166 ? -12.104 21.823  0.996   1.00 41.48  ? 280 ASN   A C   1 
ATOM   1273 O  O   . ASN   A 1 166 ? -12.046 22.113  -0.203  1.00 39.72  ? 280 ASN   A O   1 
ATOM   1274 C  CB  . ASN   A 1 166 ? -13.024 23.868  2.129   1.00 40.52  ? 280 ASN   A CB  1 
ATOM   1275 C  CG  . ASN   A 1 166 ? -11.706 24.144  2.813   1.00 41.74  ? 280 ASN   A CG  1 
ATOM   1276 O  OD1 . ASN   A 1 166 ? -11.510 23.792  3.976   1.00 45.78  ? 280 ASN   A OD1 1 
ATOM   1277 N  ND2 . ASN   A 1 166 ? -10.797 24.802  2.099   1.00 42.09  ? 280 ASN   A ND2 1 
ATOM   1278 N  N   . ALA   A 1 167 ? -11.210 21.025  1.582   1.00 41.49  ? 281 ALA   A N   1 
ATOM   1279 C  CA  . ALA   A 1 167 ? -10.144 20.408  0.802   1.00 42.86  ? 281 ALA   A CA  1 
ATOM   1280 C  C   . ALA   A 1 167 ? -10.631 19.222  -0.014  1.00 41.14  ? 281 ALA   A C   1 
ATOM   1281 O  O   . ALA   A 1 167 ? -9.925  18.784  -0.930  1.00 41.85  ? 281 ALA   A O   1 
ATOM   1282 C  CB  . ALA   A 1 167 ? -8.996  19.967  1.712   1.00 41.39  ? 281 ALA   A CB  1 
ATOM   1283 N  N   . LYS   A 1 168 ? -11.810 18.692  0.294   1.00 39.32  ? 282 LYS   A N   1 
ATOM   1284 C  CA  . LYS   A 1 168 ? -12.323 17.544  -0.432  1.00 38.62  ? 282 LYS   A CA  1 
ATOM   1285 C  C   . LYS   A 1 168 ? -13.037 18.004  -1.697  1.00 37.60  ? 282 LYS   A C   1 
ATOM   1286 O  O   . LYS   A 1 168 ? -13.896 18.890  -1.652  1.00 36.55  ? 282 LYS   A O   1 
ATOM   1287 C  CB  . LYS   A 1 168 ? -13.254 16.717  0.454   1.00 36.52  ? 282 LYS   A CB  1 
ATOM   1288 C  CG  . LYS   A 1 168 ? -12.548 16.168  1.677   1.00 40.59  ? 282 LYS   A CG  1 
ATOM   1289 C  CD  . LYS   A 1 168 ? -11.639 15.013  1.275   1.00 38.43  ? 282 LYS   A CD  1 
ATOM   1290 C  CE  . LYS   A 1 168 ? -10.904 14.447  2.476   1.00 37.93  ? 282 LYS   A CE  1 
ATOM   1291 N  NZ  . LYS   A 1 168 ? -10.354 13.095  2.178   1.00 42.24  ? 282 LYS   A NZ  1 
ATOM   1292 N  N   . THR   A 1 169 ? -12.666 17.403  -2.823  1.00 39.34  ? 283 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 169 ? -13.179 17.830  -4.116  1.00 35.80  ? 283 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 169 ? -14.658 17.490  -4.255  1.00 36.20  ? 283 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 169 ? -15.127 16.460  -3.766  1.00 35.22  ? 283 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 169 ? -12.380 17.165  -5.233  1.00 35.99  ? 283 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 169 ? -11.017 17.591  -5.146  1.00 36.57  ? 283 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 169 ? -12.922 17.550  -6.602  1.00 37.68  ? 283 THR   A CG2 1 
ATOM   1299 N  N   . ILE   A 1 170 ? -15.394 18.371  -4.925  1.00 31.51  ? 284 ILE   A N   1 
ATOM   1300 C  CA  . ILE   A 1 170 ? -16.817 18.191  -5.178  1.00 31.22  ? 284 ILE   A CA  1 
ATOM   1301 C  C   . ILE   A 1 170 ? -16.994 17.718  -6.612  1.00 30.54  ? 284 ILE   A C   1 
ATOM   1302 O  O   . ILE   A 1 170 ? -16.467 18.335  -7.546  1.00 32.61  ? 284 ILE   A O   1 
ATOM   1303 C  CB  . ILE   A 1 170 ? -17.593 19.497  -4.936  1.00 34.03  ? 284 ILE   A CB  1 
ATOM   1304 C  CG1 . ILE   A 1 170 ? -17.515 19.900  -3.466  1.00 35.05  ? 284 ILE   A CG1 1 
ATOM   1305 C  CG2 . ILE   A 1 170 ? -19.054 19.343  -5.364  1.00 36.42  ? 284 ILE   A CG2 1 
ATOM   1306 C  CD1 . ILE   A 1 170 ? -18.349 21.109  -3.126  1.00 35.35  ? 284 ILE   A CD1 1 
ATOM   1307 N  N   . ILE   A 1 171 ? -17.740 16.633  -6.796  1.00 30.27  ? 285 ILE   A N   1 
ATOM   1308 C  CA  . ILE   A 1 171 ? -18.143 16.176  -8.121  1.00 34.59  ? 285 ILE   A CA  1 
ATOM   1309 C  C   . ILE   A 1 171 ? -19.615 16.505  -8.293  1.00 35.31  ? 285 ILE   A C   1 
ATOM   1310 O  O   . ILE   A 1 171 ? -20.472 15.923  -7.615  1.00 33.38  ? 285 ILE   A O   1 
ATOM   1311 C  CB  . ILE   A 1 171 ? -17.905 14.674  -8.322  1.00 27.09  ? 285 ILE   A CB  1 
ATOM   1312 C  CG1 . ILE   A 1 171 ? -16.417 14.350  -8.282  1.00 28.31  ? 285 ILE   A CG1 1 
ATOM   1313 C  CG2 . ILE   A 1 171 ? -18.473 14.237  -9.663  1.00 30.80  ? 285 ILE   A CG2 1 
ATOM   1314 C  CD1 . ILE   A 1 171 ? -16.126 12.869  -8.376  1.00 29.57  ? 285 ILE   A CD1 1 
ATOM   1315 N  N   . VAL   A 1 172 ? -19.906 17.438  -9.188  1.00 36.01  ? 286 VAL   A N   1 
ATOM   1316 C  CA  . VAL   A 1 172 ? -21.275 17.739  -9.577  1.00 31.62  ? 286 VAL   A CA  1 
ATOM   1317 C  C   . VAL   A 1 172 ? -21.659 16.771  -10.684 1.00 34.73  ? 286 VAL   A C   1 
ATOM   1318 O  O   . VAL   A 1 172 ? -21.030 16.757  -11.745 1.00 33.56  ? 286 VAL   A O   1 
ATOM   1319 C  CB  . VAL   A 1 172 ? -21.416 19.196  -10.040 1.00 34.76  ? 286 VAL   A CB  1 
ATOM   1320 C  CG1 . VAL   A 1 172 ? -22.820 19.448  -10.557 1.00 33.38  ? 286 VAL   A CG1 1 
ATOM   1321 C  CG2 . VAL   A 1 172 ? -21.082 20.143  -8.899  1.00 32.32  ? 286 VAL   A CG2 1 
ATOM   1322 N  N   . HIS   A 1 173 ? -22.663 15.940  -10.433 1.00 32.09  ? 287 HIS   A N   1 
ATOM   1323 C  CA  . HIS   A 1 173 ? -23.194 15.037  -11.446 1.00 32.85  ? 287 HIS   A CA  1 
ATOM   1324 C  C   . HIS   A 1 173 ? -24.446 15.690  -12.020 1.00 37.12  ? 287 HIS   A C   1 
ATOM   1325 O  O   . HIS   A 1 173 ? -25.473 15.786  -11.340 1.00 36.19  ? 287 HIS   A O   1 
ATOM   1326 C  CB  . HIS   A 1 173 ? -23.504 13.660  -10.861 1.00 31.67  ? 287 HIS   A CB  1 
ATOM   1327 C  CG  . HIS   A 1 173 ? -23.546 12.562  -11.881 1.00 36.02  ? 287 HIS   A CG  1 
ATOM   1328 N  ND1 . HIS   A 1 173 ? -23.995 11.291  -11.592 1.00 31.34  ? 287 HIS   A ND1 1 
ATOM   1329 C  CD2 . HIS   A 1 173 ? -23.184 12.540  -13.186 1.00 34.57  ? 287 HIS   A CD2 1 
ATOM   1330 C  CE1 . HIS   A 1 173 ? -23.917 10.537  -12.674 1.00 33.82  ? 287 HIS   A CE1 1 
ATOM   1331 N  NE2 . HIS   A 1 173 ? -23.427 11.271  -13.657 1.00 33.16  ? 287 HIS   A NE2 1 
ATOM   1332 N  N   . LEU   A 1 174 ? -24.350 16.162  -13.258 1.00 33.49  ? 288 LEU   A N   1 
ATOM   1333 C  CA  . LEU   A 1 174 ? -25.466 16.835  -13.900 1.00 34.38  ? 288 LEU   A CA  1 
ATOM   1334 C  C   . LEU   A 1 174 ? -26.504 15.812  -14.343 1.00 39.92  ? 288 LEU   A C   1 
ATOM   1335 O  O   . LEU   A 1 174 ? -26.178 14.663  -14.651 1.00 32.70  ? 288 LEU   A O   1 
ATOM   1336 C  CB  . LEU   A 1 174 ? -24.977 17.641  -15.104 1.00 33.10  ? 288 LEU   A CB  1 
ATOM   1337 C  CG  . LEU   A 1 174 ? -23.913 18.714  -14.842 1.00 31.61  ? 288 LEU   A CG  1 
ATOM   1338 C  CD1 . LEU   A 1 174 ? -23.402 19.295  -16.155 1.00 32.25  ? 288 LEU   A CD1 1 
ATOM   1339 C  CD2 . LEU   A 1 174 ? -24.426 19.818  -13.926 1.00 29.50  ? 288 LEU   A CD2 1 
ATOM   1340 N  N   . ASN   A 1 175 ? -27.767 16.236  -14.361 1.00 38.58  ? 289 ASN   A N   1 
ATOM   1341 C  CA  . ASN   A 1 175 ? -28.836 15.398  -14.887 1.00 42.47  ? 289 ASN   A CA  1 
ATOM   1342 C  C   . ASN   A 1 175 ? -29.209 15.753  -16.316 1.00 40.72  ? 289 ASN   A C   1 
ATOM   1343 O  O   . ASN   A 1 175 ? -30.022 15.051  -16.930 1.00 42.74  ? 289 ASN   A O   1 
ATOM   1344 C  CB  . ASN   A 1 175 ? -30.076 15.477  -13.990 1.00 42.45  ? 289 ASN   A CB  1 
ATOM   1345 C  CG  . ASN   A 1 175 ? -30.608 16.888  -13.831 1.00 44.27  ? 289 ASN   A CG  1 
ATOM   1346 O  OD1 . ASN   A 1 175 ? -30.136 17.834  -14.464 1.00 44.86  ? 289 ASN   A OD1 1 
ATOM   1347 N  ND2 . ASN   A 1 175 ? -31.614 17.028  -12.981 1.00 45.51  ? 289 ASN   A ND2 1 
ATOM   1348 N  N   . LYS   A 1 176 ? -28.614 16.811  -16.853 1.00 37.95  ? 290 LYS   A N   1 
ATOM   1349 C  CA  . LYS   A 1 176 ? -28.797 17.243  -18.226 1.00 41.05  ? 290 LYS   A CA  1 
ATOM   1350 C  C   . LYS   A 1 176 ? -27.439 17.657  -18.765 1.00 41.09  ? 290 LYS   A C   1 
ATOM   1351 O  O   . LYS   A 1 176 ? -26.776 18.509  -18.170 1.00 38.98  ? 290 LYS   A O   1 
ATOM   1352 C  CB  . LYS   A 1 176 ? -29.764 18.419  -18.300 1.00 44.09  ? 290 LYS   A CB  1 
ATOM   1353 C  CG  . LYS   A 1 176 ? -30.191 18.763  -19.691 1.00 49.22  ? 290 LYS   A CG  1 
ATOM   1354 C  CD  . LYS   A 1 176 ? -31.239 19.847  -19.642 1.00 56.65  ? 290 LYS   A CD  1 
ATOM   1355 C  CE  . LYS   A 1 176 ? -31.702 20.187  -21.020 1.00 63.23  ? 290 LYS   A CE  1 
ATOM   1356 N  NZ  . LYS   A 1 176 ? -31.633 21.622  -21.363 1.00 64.12  ? 290 LYS   A NZ  1 
ATOM   1357 N  N   . SER   A 1 177 ? -27.029 17.072  -19.885 1.00 35.73  ? 291 SER   A N   1 
ATOM   1358 C  CA  . SER   A 1 177 ? -25.720 17.385  -20.435 1.00 35.96  ? 291 SER   A CA  1 
ATOM   1359 C  C   . SER   A 1 177 ? -25.750 18.726  -21.159 1.00 43.29  ? 291 SER   A C   1 
ATOM   1360 O  O   . SER   A 1 177 ? -26.784 19.162  -21.674 1.00 41.19  ? 291 SER   A O   1 
ATOM   1361 C  CB  . SER   A 1 177 ? -25.246 16.288  -21.387 1.00 41.93  ? 291 SER   A CB  1 
ATOM   1362 O  OG  . SER   A 1 177 ? -26.028 16.267  -22.566 1.00 47.48  ? 291 SER   A OG  1 
ATOM   1363 N  N   . VAL   A 1 178 ? -24.597 19.385  -21.188 1.00 36.77  ? 292 VAL   A N   1 
ATOM   1364 C  CA  . VAL   A 1 178 ? -24.416 20.642  -21.901 1.00 36.08  ? 292 VAL   A CA  1 
ATOM   1365 C  C   . VAL   A 1 178 ? -23.320 20.425  -22.931 1.00 37.18  ? 292 VAL   A C   1 
ATOM   1366 O  O   . VAL   A 1 178 ? -22.174 20.129  -22.571 1.00 34.47  ? 292 VAL   A O   1 
ATOM   1367 C  CB  . VAL   A 1 178 ? -24.059 21.791  -20.947 1.00 37.72  ? 292 VAL   A CB  1 
ATOM   1368 C  CG1 . VAL   A 1 178 ? -23.735 23.045  -21.733 1.00 41.10  ? 292 VAL   A CG1 1 
ATOM   1369 C  CG2 . VAL   A 1 178 ? -25.205 22.045  -19.988 1.00 39.47  ? 292 VAL   A CG2 1 
ATOM   1370 N  N   . GLU   A 1 179 ? -23.670 20.561  -24.204 1.00 39.19  ? 293 GLU   A N   1 
ATOM   1371 C  CA  . GLU   A 1 179 ? -22.716 20.309  -25.273 1.00 36.02  ? 293 GLU   A CA  1 
ATOM   1372 C  C   . GLU   A 1 179 ? -21.593 21.344  -25.244 1.00 35.90  ? 293 GLU   A C   1 
ATOM   1373 O  O   . GLU   A 1 179 ? -21.814 22.515  -24.925 1.00 33.71  ? 293 GLU   A O   1 
ATOM   1374 C  CB  . GLU   A 1 179 ? -23.430 20.338  -26.621 1.00 38.04  ? 293 GLU   A CB  1 
ATOM   1375 C  CG  . GLU   A 1 179 ? -22.753 19.558  -27.713 1.00 42.79  ? 293 GLU   A CG  1 
ATOM   1376 C  CD  . GLU   A 1 179 ? -23.746 19.057  -28.745 1.00 50.46  ? 293 GLU   A CD  1 
ATOM   1377 O  OE1 . GLU   A 1 179 ? -24.540 19.881  -29.250 1.00 54.30  ? 293 GLU   A OE1 1 
ATOM   1378 O  OE2 . GLU   A 1 179 ? -23.738 17.845  -29.057 1.00 50.39  ? 293 GLU   A OE2 1 
ATOM   1379 N  N   . ILE   A 1 180 ? -20.376 20.903  -25.558 1.00 33.34  ? 294 ILE   A N   1 
ATOM   1380 C  CA  . ILE   A 1 180 ? -19.233 21.800  -25.712 1.00 29.92  ? 294 ILE   A CA  1 
ATOM   1381 C  C   . ILE   A 1 180 ? -18.522 21.401  -27.001 1.00 33.56  ? 294 ILE   A C   1 
ATOM   1382 O  O   . ILE   A 1 180 ? -18.017 20.279  -27.119 1.00 33.73  ? 294 ILE   A O   1 
ATOM   1383 C  CB  . ILE   A 1 180 ? -18.276 21.774  -24.504 1.00 31.68  ? 294 ILE   A CB  1 
ATOM   1384 C  CG1 . ILE   A 1 180 ? -17.113 22.748  -24.718 1.00 30.15  ? 294 ILE   A CG1 1 
ATOM   1385 C  CG2 . ILE   A 1 180 ? -17.806 20.353  -24.169 1.00 30.71  ? 294 ILE   A CG2 1 
ATOM   1386 C  CD1 . ILE   A 1 180 ? -16.297 22.996  -23.483 1.00 31.65  ? 294 ILE   A CD1 1 
ATOM   1387 N  N   . ASN   A 1 181 ? -18.527 22.296  -27.982 1.00 33.27  ? 295 ASN   A N   1 
ATOM   1388 C  CA  . ASN   A 1 181 ? -18.087 22.003  -29.340 1.00 33.45  ? 295 ASN   A CA  1 
ATOM   1389 C  C   . ASN   A 1 181 ? -16.766 22.725  -29.569 1.00 36.44  ? 295 ASN   A C   1 
ATOM   1390 O  O   . ASN   A 1 181 ? -16.737 23.953  -29.700 1.00 33.86  ? 295 ASN   A O   1 
ATOM   1391 C  CB  . ASN   A 1 181 ? -19.157 22.432  -30.340 1.00 37.55  ? 295 ASN   A CB  1 
ATOM   1392 C  CG  . ASN   A 1 181 ? -18.711 22.306  -31.775 1.00 41.78  ? 295 ASN   A CG  1 
ATOM   1393 O  OD1 . ASN   A 1 181 ? -17.666 21.734  -32.084 1.00 40.12  ? 295 ASN   A OD1 1 
ATOM   1394 N  ND2 . ASN   A 1 181 ? -19.509 22.861  -32.669 1.00 47.71  ? 295 ASN   A ND2 1 
ATOM   1395 N  N   . CYS   A 1 182 ? -15.681 21.961  -29.622 1.00 30.75  ? 296 CYS   A N   1 
ATOM   1396 C  CA  . CYS   A 1 182 ? -14.332 22.504  -29.632 1.00 31.70  ? 296 CYS   A CA  1 
ATOM   1397 C  C   . CYS   A 1 182 ? -13.690 22.263  -30.989 1.00 32.15  ? 296 CYS   A C   1 
ATOM   1398 O  O   . CYS   A 1 182 ? -13.720 21.142  -31.504 1.00 33.63  ? 296 CYS   A O   1 
ATOM   1399 C  CB  . CYS   A 1 182 ? -13.501 21.868  -28.520 1.00 34.63  ? 296 CYS   A CB  1 
ATOM   1400 S  SG  . CYS   A 1 182 ? -14.246 22.127  -26.905 1.00 34.58  ? 296 CYS   A SG  1 
ATOM   1401 N  N   . THR   A 1 183 ? -13.103 23.309  -31.560 1.00 32.53  ? 297 THR   A N   1 
ATOM   1402 C  CA  . THR   A 1 183 ? -12.564 23.221  -32.905 1.00 30.23  ? 297 THR   A CA  1 
ATOM   1403 C  C   . THR   A 1 183 ? -11.237 23.954  -33.000 1.00 33.85  ? 297 THR   A C   1 
ATOM   1404 O  O   . THR   A 1 183 ? -11.121 25.104  -32.570 1.00 34.51  ? 297 THR   A O   1 
ATOM   1405 C  CB  . THR   A 1 183 ? -13.543 23.811  -33.924 1.00 36.01  ? 297 THR   A CB  1 
ATOM   1406 O  OG1 . THR   A 1 183 ? -14.781 23.092  -33.881 1.00 36.59  ? 297 THR   A OG1 1 
ATOM   1407 C  CG2 . THR   A 1 183 ? -12.962 23.748  -35.318 1.00 37.36  ? 297 THR   A CG2 1 
ATOM   1408 N  N   . ARG   A 1 184 ? -10.242 23.286  -33.580 1.00 30.33  ? 298 ARG   A N   1 
ATOM   1409 C  CA  . ARG   A 1 184 ? -9.058  23.974  -34.080 1.00 31.76  ? 298 ARG   A CA  1 
ATOM   1410 C  C   . ARG   A 1 184 ? -9.269  24.043  -35.585 1.00 35.19  ? 298 ARG   A C   1 
ATOM   1411 O  O   . ARG   A 1 184 ? -9.122  23.022  -36.275 1.00 34.44  ? 298 ARG   A O   1 
ATOM   1412 C  CB  . ARG   A 1 184 ? -7.768  23.211  -33.753 1.00 29.89  ? 298 ARG   A CB  1 
ATOM   1413 C  CG  . ARG   A 1 184 ? -6.458  23.974  -33.967 1.00 30.58  ? 298 ARG   A CG  1 
ATOM   1414 C  CD  . ARG   A 1 184 ? -6.174  24.321  -35.434 1.00 29.95  ? 298 ARG   A CD  1 
ATOM   1415 N  NE  . ARG   A 1 184 ? -6.108  23.172  -36.331 1.00 29.70  ? 298 ARG   A NE  1 
ATOM   1416 C  CZ  . ARG   A 1 184 ? -4.996  22.519  -36.642 1.00 29.52  ? 298 ARG   A CZ  1 
ATOM   1417 N  NH1 . ARG   A 1 184 ? -3.829  22.852  -36.118 1.00 35.85  ? 298 ARG   A NH1 1 
ATOM   1418 N  NH2 . ARG   A 1 184 ? -5.055  21.516  -37.514 1.00 38.93  ? 298 ARG   A NH2 1 
ATOM   1419 N  N   . PRO   A 1 185 ? -9.602  25.203  -36.145 1.00 36.45  ? 299 PRO   A N   1 
ATOM   1420 C  CA  . PRO   A 1 185 ? -9.901  25.265  -37.579 1.00 40.74  ? 299 PRO   A CA  1 
ATOM   1421 C  C   . PRO   A 1 185 ? -8.679  24.974  -38.446 1.00 37.80  ? 299 PRO   A C   1 
ATOM   1422 O  O   . PRO   A 1 185 ? -7.532  25.147  -38.028 1.00 41.18  ? 299 PRO   A O   1 
ATOM   1423 C  CB  . PRO   A 1 185 ? -10.403 26.701  -37.775 1.00 35.22  ? 299 PRO   A CB  1 
ATOM   1424 C  CG  . PRO   A 1 185 ? -9.859  27.456  -36.627 1.00 39.70  ? 299 PRO   A CG  1 
ATOM   1425 C  CD  . PRO   A 1 185 ? -9.781  26.504  -35.482 1.00 32.75  ? 299 PRO   A CD  1 
ATOM   1426 N  N   . SER   A 1 186 ? -8.950  24.550  -39.681 1.00 41.31  ? 300 SER   A N   1 
ATOM   1427 C  CA  . SER   A 1 186 ? -7.916  24.019  -40.560 1.00 41.46  ? 300 SER   A CA  1 
ATOM   1428 C  C   . SER   A 1 186 ? -6.975  25.128  -41.042 1.00 48.92  ? 300 SER   A C   1 
ATOM   1429 O  O   . SER   A 1 186 ? -7.271  26.323  -40.945 1.00 47.76  ? 300 SER   A O   1 
ATOM   1430 C  CB  . SER   A 1 186 ? -8.552  23.299  -41.748 1.00 43.05  ? 300 SER   A CB  1 
ATOM   1431 O  OG  . SER   A 1 186 ? -9.816  23.858  -42.073 1.00 50.65  ? 300 SER   A OG  1 
ATOM   1432 N  N   . ASN   A 1 187 ? -5.819  24.704  -41.558 1.00 59.99  ? 301 ASN   A N   1 
ATOM   1433 C  CA  . ASN   A 1 187 ? -4.776  25.571  -42.126 1.00 61.40  ? 301 ASN   A CA  1 
ATOM   1434 C  C   . ASN   A 1 187 ? -4.092  26.450  -41.097 1.00 64.39  ? 301 ASN   A C   1 
ATOM   1435 O  O   . ASN   A 1 187 ? -3.018  27.001  -41.368 1.00 77.52  ? 301 ASN   A O   1 
ATOM   1436 C  CB  . ASN   A 1 187 ? -5.330  26.460  -43.243 1.00 63.53  ? 301 ASN   A CB  1 
ATOM   1437 C  CG  . ASN   A 1 187 ? -5.657  25.679  -44.490 1.00 68.22  ? 301 ASN   A CG  1 
ATOM   1438 O  OD1 . ASN   A 1 187 ? -4.754  25.292  -45.231 1.00 85.06  ? 301 ASN   A OD1 1 
ATOM   1439 N  ND2 . ASN   A 1 187 ? -6.946  25.467  -44.752 1.00 68.22  ? 301 ASN   A ND2 1 
ATOM   1440 N  N   . ASP   A 1 195 ? -2.328  31.057  -36.288 1.00 53.99  ? 325 ASP   A N   1 
ATOM   1441 C  CA  . ASP   A 1 195 ? -1.877  30.391  -35.076 1.00 47.93  ? 325 ASP   A CA  1 
ATOM   1442 C  C   . ASP   A 1 195 ? -2.497  29.006  -35.001 1.00 47.73  ? 325 ASP   A C   1 
ATOM   1443 O  O   . ASP   A 1 195 ? -3.635  28.854  -34.558 1.00 49.62  ? 325 ASP   A O   1 
ATOM   1444 C  CB  . ASP   A 1 195 ? -2.249  31.223  -33.845 1.00 49.44  ? 325 ASP   A CB  1 
ATOM   1445 C  CG  . ASP   A 1 195 ? -1.583  30.728  -32.571 1.00 49.53  ? 325 ASP   A CG  1 
ATOM   1446 O  OD1 . ASP   A 1 195 ? -0.959  29.643  -32.587 1.00 47.12  ? 325 ASP   A OD1 1 
ATOM   1447 O  OD2 . ASP   A 1 195 ? -1.687  31.430  -31.539 1.00 53.69  ? 325 ASP   A OD2 1 
ATOM   1448 N  N   . ILE   A 1 196 ? -1.743  27.991  -35.432 1.00 44.04  ? 326 ILE   A N   1 
ATOM   1449 C  CA  . ILE   A 1 196 ? -2.280  26.639  -35.528 1.00 44.20  ? 326 ILE   A CA  1 
ATOM   1450 C  C   . ILE   A 1 196 ? -2.645  26.048  -34.173 1.00 38.45  ? 326 ILE   A C   1 
ATOM   1451 O  O   . ILE   A 1 196 ? -3.306  25.006  -34.116 1.00 43.21  ? 326 ILE   A O   1 
ATOM   1452 C  CB  . ILE   A 1 196 ? -1.291  25.695  -36.251 1.00 42.54  ? 326 ILE   A CB  1 
ATOM   1453 C  CG1 . ILE   A 1 196 ? 0.033   25.602  -35.487 1.00 45.93  ? 326 ILE   A CG1 1 
ATOM   1454 C  CG2 . ILE   A 1 196 ? -1.078  26.147  -37.685 1.00 48.22  ? 326 ILE   A CG2 1 
ATOM   1455 C  CD1 . ILE   A 1 196 ? 1.056   24.696  -36.136 1.00 47.02  ? 326 ILE   A CD1 1 
ATOM   1456 N  N   . ARG   A 1 197 ? -2.233  26.680  -33.074 1.00 35.28  ? 327 ARG   A N   1 
ATOM   1457 C  CA  . ARG   A 1 197 ? -2.600  26.198  -31.750 1.00 32.70  ? 327 ARG   A CA  1 
ATOM   1458 C  C   . ARG   A 1 197 ? -3.839  26.886  -31.196 1.00 35.74  ? 327 ARG   A C   1 
ATOM   1459 O  O   . ARG   A 1 197 ? -4.390  26.424  -30.192 1.00 31.14  ? 327 ARG   A O   1 
ATOM   1460 C  CB  . ARG   A 1 197 ? -1.432  26.382  -30.777 1.00 31.33  ? 327 ARG   A CB  1 
ATOM   1461 C  CG  . ARG   A 1 197 ? -0.112  25.831  -31.303 1.00 32.77  ? 327 ARG   A CG  1 
ATOM   1462 C  CD  . ARG   A 1 197 ? 0.966   25.844  -30.228 1.00 38.70  ? 327 ARG   A CD  1 
ATOM   1463 N  NE  . ARG   A 1 197 ? 2.166   25.107  -30.611 1.00 35.78  ? 327 ARG   A NE  1 
ATOM   1464 C  CZ  . ARG   A 1 197 ? 2.955   25.425  -31.631 1.00 42.00  ? 327 ARG   A CZ  1 
ATOM   1465 N  NH1 . ARG   A 1 197 ? 2.703   26.467  -32.409 1.00 38.53  ? 327 ARG   A NH1 1 
ATOM   1466 N  NH2 . ARG   A 1 197 ? 4.034   24.686  -31.869 1.00 36.40  ? 327 ARG   A NH2 1 
ATOM   1467 N  N   . LYS   A 1 198 ? -4.296  27.962  -31.832 1.00 35.06  ? 328 LYS   A N   1 
ATOM   1468 C  CA  . LYS   A 1 198 ? -5.493  28.649  -31.372 1.00 31.41  ? 328 LYS   A CA  1 
ATOM   1469 C  C   . LYS   A 1 198 ? -6.721  27.820  -31.713 1.00 29.64  ? 328 LYS   A C   1 
ATOM   1470 O  O   . LYS   A 1 198 ? -6.885  27.371  -32.849 1.00 28.72  ? 328 LYS   A O   1 
ATOM   1471 C  CB  . LYS   A 1 198 ? -5.603  30.033  -32.010 1.00 35.30  ? 328 LYS   A CB  1 
ATOM   1472 C  CG  . LYS   A 1 198 ? -6.690  30.921  -31.384 1.00 40.18  ? 328 LYS   A CG  1 
ATOM   1473 C  CD  . LYS   A 1 198 ? -6.376  31.203  -29.917 1.00 46.27  ? 328 LYS   A CD  1 
ATOM   1474 C  CE  . LYS   A 1 198 ? -7.574  31.025  -28.980 1.00 37.64  ? 328 LYS   A CE  1 
ATOM   1475 N  NZ  . LYS   A 1 198 ? -8.896  31.452  -29.512 1.00 37.05  ? 328 LYS   A NZ  1 
ATOM   1476 N  N   . ALA   A 1 199 ? -7.582  27.611  -30.724 1.00 30.00  ? 329 ALA   A N   1 
ATOM   1477 C  CA  . ALA   A 1 199 ? -8.818  26.872  -30.917 1.00 32.31  ? 329 ALA   A CA  1 
ATOM   1478 C  C   . ALA   A 1 199 ? -9.889  27.541  -30.071 1.00 34.13  ? 329 ALA   A C   1 
ATOM   1479 O  O   . ALA   A 1 199 ? -9.632  28.526  -29.373 1.00 31.75  ? 329 ALA   A O   1 
ATOM   1480 C  CB  . ALA   A 1 199 ? -8.652  25.390  -30.559 1.00 32.16  ? 329 ALA   A CB  1 
ATOM   1481 N  N   . TYR   A 1 200 ? -11.098 26.998  -30.117 1.00 34.43  ? 330 TYR   A N   1 
ATOM   1482 C  CA  . TYR   A 1 200 ? -12.174 27.575  -29.328 1.00 36.78  ? 330 TYR   A CA  1 
ATOM   1483 C  C   . TYR   A 1 200 ? -13.231 26.509  -29.109 1.00 36.93  ? 330 TYR   A C   1 
ATOM   1484 O  O   . TYR   A 1 200 ? -13.415 25.622  -29.946 1.00 35.60  ? 330 TYR   A O   1 
ATOM   1485 C  CB  . TYR   A 1 200 ? -12.790 28.794  -30.023 1.00 39.72  ? 330 TYR   A CB  1 
ATOM   1486 C  CG  . TYR   A 1 200 ? -13.384 28.443  -31.360 1.00 43.99  ? 330 TYR   A CG  1 
ATOM   1487 C  CD1 . TYR   A 1 200 ? -12.614 28.476  -32.509 1.00 39.48  ? 330 TYR   A CD1 1 
ATOM   1488 C  CD2 . TYR   A 1 200 ? -14.718 28.071  -31.470 1.00 44.82  ? 330 TYR   A CD2 1 
ATOM   1489 C  CE1 . TYR   A 1 200 ? -13.148 28.140  -33.730 1.00 46.63  ? 330 TYR   A CE1 1 
ATOM   1490 C  CE2 . TYR   A 1 200 ? -15.262 27.737  -32.687 1.00 46.65  ? 330 TYR   A CE2 1 
ATOM   1491 C  CZ  . TYR   A 1 200 ? -14.475 27.777  -33.815 1.00 46.62  ? 330 TYR   A CZ  1 
ATOM   1492 O  OH  . TYR   A 1 200 ? -15.024 27.445  -35.031 1.00 50.26  ? 330 TYR   A OH  1 
ATOM   1493 N  N   . CYS   A 1 201 ? -13.916 26.602  -27.977 1.00 37.72  ? 331 CYS   A N   1 
ATOM   1494 C  CA  . CYS   A 1 201 ? -15.059 25.753  -27.681 1.00 35.70  ? 331 CYS   A CA  1 
ATOM   1495 C  C   . CYS   A 1 201 ? -16.311 26.612  -27.664 1.00 33.83  ? 331 CYS   A C   1 
ATOM   1496 O  O   . CYS   A 1 201 ? -16.342 27.658  -27.010 1.00 37.48  ? 331 CYS   A O   1 
ATOM   1497 C  CB  . CYS   A 1 201 ? -14.887 25.034  -26.344 1.00 36.46  ? 331 CYS   A CB  1 
ATOM   1498 S  SG  . CYS   A 1 201 ? -13.492 23.913  -26.313 1.00 39.35  ? 331 CYS   A SG  1 
ATOM   1499 N  N   . GLU   A 1 202 ? -17.326 26.182  -28.398 1.00 29.73  ? 332 GLU   A N   1 
ATOM   1500 C  CA  . GLU   A 1 202 ? -18.607 26.865  -28.429 1.00 35.22  ? 332 GLU   A CA  1 
ATOM   1501 C  C   . GLU   A 1 202 ? -19.544 26.170  -27.455 1.00 35.33  ? 332 GLU   A C   1 
ATOM   1502 O  O   . GLU   A 1 202 ? -19.650 24.938  -27.457 1.00 35.70  ? 332 GLU   A O   1 
ATOM   1503 C  CB  . GLU   A 1 202 ? -19.188 26.856  -29.842 1.00 37.56  ? 332 GLU   A CB  1 
ATOM   1504 C  CG  . GLU   A 1 202 ? -18.296 27.549  -30.867 1.00 42.35  ? 332 GLU   A CG  1 
ATOM   1505 C  CD  . GLU   A 1 202 ? -19.075 28.172  -32.011 1.00 47.08  ? 332 GLU   A CD  1 
ATOM   1506 O  OE1 . GLU   A 1 202 ? -20.095 27.582  -32.431 1.00 49.78  ? 332 GLU   A OE1 1 
ATOM   1507 O  OE2 . GLU   A 1 202 ? -18.658 29.242  -32.508 1.00 49.88  ? 332 GLU   A OE2 1 
ATOM   1508 N  N   . ILE   A 1 203 ? -20.195 26.955  -26.608 1.00 35.93  ? 333 ILE   A N   1 
ATOM   1509 C  CA  . ILE   A 1 203 ? -21.162 26.447  -25.647 1.00 35.68  ? 333 ILE   A CA  1 
ATOM   1510 C  C   . ILE   A 1 203 ? -22.385 27.341  -25.710 1.00 39.16  ? 333 ILE   A C   1 
ATOM   1511 O  O   . ILE   A 1 203 ? -22.265 28.569  -25.777 1.00 34.15  ? 333 ILE   A O   1 
ATOM   1512 C  CB  . ILE   A 1 203 ? -20.597 26.416  -24.212 1.00 40.24  ? 333 ILE   A CB  1 
ATOM   1513 C  CG1 . ILE   A 1 203 ? -19.454 25.418  -24.116 1.00 39.51  ? 333 ILE   A CG1 1 
ATOM   1514 C  CG2 . ILE   A 1 203 ? -21.675 26.020  -23.219 1.00 40.32  ? 333 ILE   A CG2 1 
ATOM   1515 C  CD1 . ILE   A 1 203 ? -18.426 25.812  -23.112 1.00 36.00  ? 333 ILE   A CD1 1 
ATOM   1516 N  N   . ASN   A 1 204 ? -23.561 26.730  -25.700 1.00 36.87  ? 334 ASN   A N   1 
ATOM   1517 C  CA  . ASN   A 1 204 ? -24.783 27.512  -25.759 1.00 38.02  ? 334 ASN   A CA  1 
ATOM   1518 C  C   . ASN   A 1 204 ? -24.988 28.147  -24.389 1.00 38.15  ? 334 ASN   A C   1 
ATOM   1519 O  O   . ASN   A 1 204 ? -25.231 27.444  -23.401 1.00 36.78  ? 334 ASN   A O   1 
ATOM   1520 C  CB  . ASN   A 1 204 ? -25.944 26.614  -26.172 1.00 41.31  ? 334 ASN   A CB  1 
ATOM   1521 C  CG  . ASN   A 1 204 ? -27.303 27.271  -26.016 1.00 44.42  ? 334 ASN   A CG  1 
ATOM   1522 O  OD1 . ASN   A 1 204 ? -27.492 28.250  -25.298 1.00 42.42  ? 334 ASN   A OD1 1 
ATOM   1523 N  ND2 . ASN   A 1 204 ? -28.263 26.729  -26.729 1.00 46.69  ? 334 ASN   A ND2 1 
ATOM   1524 N  N   . GLY   A 1 205 ? -24.889 29.482  -24.333 1.00 38.19  ? 335 GLY   A N   1 
ATOM   1525 C  CA  . GLY   A 1 205 ? -24.948 30.171  -23.057 1.00 36.10  ? 335 GLY   A CA  1 
ATOM   1526 C  C   . GLY   A 1 205 ? -26.294 30.063  -22.374 1.00 42.26  ? 335 GLY   A C   1 
ATOM   1527 O  O   . GLY   A 1 205 ? -26.370 30.106  -21.142 1.00 39.68  ? 335 GLY   A O   1 
ATOM   1528 N  N   . THR   A 1 206 ? -27.372 29.927  -23.155 1.00 42.65  ? 336 THR   A N   1 
ATOM   1529 C  CA  . THR   A 1 206 ? -28.688 29.711  -22.562 1.00 44.35  ? 336 THR   A CA  1 
ATOM   1530 C  C   . THR   A 1 206 ? -28.698 28.441  -21.728 1.00 40.86  ? 336 THR   A C   1 
ATOM   1531 O  O   . THR   A 1 206 ? -29.056 28.461  -20.545 1.00 42.38  ? 336 THR   A O   1 
ATOM   1532 C  CB  . THR   A 1 206 ? -29.761 29.642  -23.645 1.00 44.86  ? 336 THR   A CB  1 
ATOM   1533 O  OG1 . THR   A 1 206 ? -29.893 30.928  -24.259 1.00 54.03  ? 336 THR   A OG1 1 
ATOM   1534 C  CG2 . THR   A 1 206 ? -31.102 29.245  -23.032 1.00 45.21  ? 336 THR   A CG2 1 
ATOM   1535 N  N   . LYS   A 1 207 ? -28.290 27.327  -22.333 1.00 42.76  ? 337 LYS   A N   1 
ATOM   1536 C  CA  . LYS   A 1 207 ? -28.222 26.054  -21.630 1.00 41.16  ? 337 LYS   A CA  1 
ATOM   1537 C  C   . LYS   A 1 207 ? -27.304 26.129  -20.415 1.00 41.03  ? 337 LYS   A C   1 
ATOM   1538 O  O   . LYS   A 1 207 ? -27.713 25.814  -19.291 1.00 44.40  ? 337 LYS   A O   1 
ATOM   1539 C  CB  . LYS   A 1 207 ? -27.740 24.987  -22.598 1.00 46.90  ? 337 LYS   A CB  1 
ATOM   1540 C  CG  . LYS   A 1 207 ? -28.794 24.469  -23.535 1.00 53.52  ? 337 LYS   A CG  1 
ATOM   1541 C  CD  . LYS   A 1 207 ? -28.306 23.156  -24.099 1.00 51.84  ? 337 LYS   A CD  1 
ATOM   1542 C  CE  . LYS   A 1 207 ? -26.834 23.299  -24.490 1.00 57.12  ? 337 LYS   A CE  1 
ATOM   1543 N  NZ  . LYS   A 1 207 ? -26.200 22.039  -24.900 1.00 58.40  ? 337 LYS   A NZ  1 
ATOM   1544 N  N   . TRP   A 1 208 ? -26.049 26.540  -20.626 1.00 39.05  ? 338 TRP   A N   1 
ATOM   1545 C  CA  . TRP   A 1 208 ? -25.059 26.516  -19.550 1.00 41.75  ? 338 TRP   A CA  1 
ATOM   1546 C  C   . TRP   A 1 208 ? -25.515 27.296  -18.325 1.00 41.99  ? 338 TRP   A C   1 
ATOM   1547 O  O   . TRP   A 1 208 ? -25.417 26.809  -17.192 1.00 40.83  ? 338 TRP   A O   1 
ATOM   1548 C  CB  . TRP   A 1 208 ? -23.723 27.065  -20.043 1.00 36.85  ? 338 TRP   A CB  1 
ATOM   1549 C  CG  . TRP   A 1 208 ? -22.761 27.250  -18.918 1.00 38.35  ? 338 TRP   A CG  1 
ATOM   1550 C  CD1 . TRP   A 1 208 ? -22.376 28.431  -18.360 1.00 37.47  ? 338 TRP   A CD1 1 
ATOM   1551 C  CD2 . TRP   A 1 208 ? -22.106 26.221  -18.172 1.00 36.43  ? 338 TRP   A CD2 1 
ATOM   1552 N  NE1 . TRP   A 1 208 ? -21.498 28.205  -17.330 1.00 42.08  ? 338 TRP   A NE1 1 
ATOM   1553 C  CE2 . TRP   A 1 208 ? -21.316 26.855  -17.193 1.00 38.97  ? 338 TRP   A CE2 1 
ATOM   1554 C  CE3 . TRP   A 1 208 ? -22.098 24.825  -18.245 1.00 39.52  ? 338 TRP   A CE3 1 
ATOM   1555 C  CZ2 . TRP   A 1 208 ? -20.529 26.143  -16.295 1.00 41.95  ? 338 TRP   A CZ2 1 
ATOM   1556 C  CZ3 . TRP   A 1 208 ? -21.317 24.119  -17.353 1.00 36.18  ? 338 TRP   A CZ3 1 
ATOM   1557 C  CH2 . TRP   A 1 208 ? -20.542 24.779  -16.391 1.00 37.14  ? 338 TRP   A CH2 1 
ATOM   1558 N  N   . ASN   A 1 209 ? -25.993 28.524  -18.529 1.00 41.83  ? 339 ASN   A N   1 
ATOM   1559 C  CA  . ASN   A 1 209 ? -26.366 29.359  -17.394 1.00 42.02  ? 339 ASN   A CA  1 
ATOM   1560 C  C   . ASN   A 1 209 ? -27.601 28.809  -16.699 1.00 41.42  ? 339 ASN   A C   1 
ATOM   1561 O  O   . ASN   A 1 209 ? -27.776 29.002  -15.489 1.00 41.59  ? 339 ASN   A O   1 
ATOM   1562 C  CB  . ASN   A 1 209 ? -26.594 30.791  -17.865 1.00 46.56  ? 339 ASN   A CB  1 
ATOM   1563 C  CG  . ASN   A 1 209 ? -25.308 31.482  -18.249 1.00 48.57  ? 339 ASN   A CG  1 
ATOM   1564 O  OD1 . ASN   A 1 209 ? -24.276 31.307  -17.600 1.00 48.24  ? 339 ASN   A OD1 1 
ATOM   1565 N  ND2 . ASN   A 1 209 ? -25.353 32.255  -19.331 1.00 51.53  ? 339 ASN   A ND2 1 
ATOM   1566 N  N   . LYS   A 1 210 ? -28.453 28.103  -17.446 1.00 40.78  ? 340 LYS   A N   1 
ATOM   1567 C  CA  . LYS   A 1 210 ? -29.562 27.378  -16.838 1.00 45.29  ? 340 LYS   A CA  1 
ATOM   1568 C  C   . LYS   A 1 210 ? -29.038 26.281  -15.921 1.00 43.27  ? 340 LYS   A C   1 
ATOM   1569 O  O   . LYS   A 1 210 ? -29.382 26.225  -14.733 1.00 40.58  ? 340 LYS   A O   1 
ATOM   1570 C  CB  . LYS   A 1 210 ? -30.455 26.800  -17.940 1.00 45.96  ? 340 LYS   A CB  1 
ATOM   1571 C  CG  . LYS   A 1 210 ? -31.702 26.077  -17.453 1.00 54.88  ? 340 LYS   A CG  1 
ATOM   1572 C  CD  . LYS   A 1 210 ? -32.519 26.967  -16.541 1.00 58.20  ? 340 LYS   A CD  1 
ATOM   1573 C  CE  . LYS   A 1 210 ? -33.854 26.334  -16.206 1.00 58.82  ? 340 LYS   A CE  1 
ATOM   1574 N  NZ  . LYS   A 1 210 ? -34.402 25.607  -17.379 1.00 62.12  ? 340 LYS   A NZ  1 
ATOM   1575 N  N   . VAL   A 1 211 ? -28.168 25.422  -16.458 1.00 38.37  ? 341 VAL   A N   1 
ATOM   1576 C  CA  . VAL   A 1 211 ? -27.587 24.330  -15.683 1.00 40.24  ? 341 VAL   A CA  1 
ATOM   1577 C  C   . VAL   A 1 211 ? -26.760 24.868  -14.525 1.00 39.24  ? 341 VAL   A C   1 
ATOM   1578 O  O   . VAL   A 1 211 ? -26.844 24.363  -13.398 1.00 43.16  ? 341 VAL   A O   1 
ATOM   1579 C  CB  . VAL   A 1 211 ? -26.753 23.423  -16.606 1.00 43.03  ? 341 VAL   A CB  1 
ATOM   1580 C  CG1 . VAL   A 1 211 ? -25.783 22.575  -15.801 1.00 43.35  ? 341 VAL   A CG1 1 
ATOM   1581 C  CG2 . VAL   A 1 211 ? -27.668 22.540  -17.418 1.00 39.98  ? 341 VAL   A CG2 1 
ATOM   1582 N  N   . LEU   A 1 212 ? -25.945 25.897  -14.779 1.00 38.54  ? 342 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 212 ? -25.165 26.488  -13.696 1.00 42.95  ? 342 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 212 ? -26.068 27.045  -12.603 1.00 44.73  ? 342 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 212 ? -25.758 26.926  -11.411 1.00 44.32  ? 342 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 212 ? -24.244 27.581  -14.231 1.00 42.68  ? 342 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 212 ? -23.106 27.893  -13.255 1.00 43.77  ? 342 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 212 ? -22.320 26.629  -12.945 1.00 42.01  ? 342 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 212 ? -22.192 28.990  -13.777 1.00 42.00  ? 342 LEU   A CD2 1 
ATOM   1590 N  N   . LYS   A 1 213 ? -27.190 27.662  -12.988 1.00 42.05  ? 343 LYS   A N   1 
ATOM   1591 C  CA  . LYS   A 1 213 ? -28.134 28.154  -11.991 1.00 43.95  ? 343 LYS   A CA  1 
ATOM   1592 C  C   . LYS   A 1 213 ? -28.690 27.004  -11.159 1.00 43.05  ? 343 LYS   A C   1 
ATOM   1593 O  O   . LYS   A 1 213 ? -28.815 27.115  -9.932  1.00 45.59  ? 343 LYS   A O   1 
ATOM   1594 C  CB  . LYS   A 1 213 ? -29.265 28.922  -12.674 1.00 43.84  ? 343 LYS   A CB  1 
ATOM   1595 C  CG  . LYS   A 1 213 ? -30.438 29.259  -11.748 1.00 47.55  ? 343 LYS   A CG  1 
ATOM   1596 C  CD  . LYS   A 1 213 ? -31.576 29.976  -12.479 1.00 51.98  ? 343 LYS   A CD  1 
ATOM   1597 C  CE  . LYS   A 1 213 ? -32.110 29.211  -13.687 1.00 62.14  ? 343 LYS   A CE  1 
ATOM   1598 N  NZ  . LYS   A 1 213 ? -31.863 27.743  -13.640 1.00 75.03  ? 343 LYS   A NZ  1 
ATOM   1599 N  N   . GLN   A 1 214 ? -29.007 25.880  -11.809 1.00 41.60  ? 344 GLN   A N   1 
ATOM   1600 C  CA  . GLN   A 1 214 ? -29.485 24.710  -11.081 1.00 40.55  ? 344 GLN   A CA  1 
ATOM   1601 C  C   . GLN   A 1 214 ? -28.412 24.179  -10.136 1.00 44.27  ? 344 GLN   A C   1 
ATOM   1602 O  O   . GLN   A 1 214 ? -28.716 23.747  -9.016  1.00 41.73  ? 344 GLN   A O   1 
ATOM   1603 C  CB  . GLN   A 1 214 ? -29.940 23.636  -12.071 1.00 40.96  ? 344 GLN   A CB  1 
ATOM   1604 C  CG  . GLN   A 1 214 ? -31.152 24.063  -12.901 1.00 42.87  ? 344 GLN   A CG  1 
ATOM   1605 C  CD  . GLN   A 1 214 ? -31.676 22.977  -13.824 1.00 45.73  ? 344 GLN   A CD  1 
ATOM   1606 O  OE1 . GLN   A 1 214 ? -31.122 21.879  -13.898 1.00 50.81  ? 344 GLN   A OE1 1 
ATOM   1607 N  NE2 . GLN   A 1 214 ? -32.757 23.284  -14.540 1.00 49.09  ? 344 GLN   A NE2 1 
ATOM   1608 N  N   . VAL   A 1 215 ? -27.145 24.236  -10.558 1.00 41.08  ? 345 VAL   A N   1 
ATOM   1609 C  CA  . VAL   A 1 215 ? -26.045 23.807  -9.696  1.00 40.11  ? 345 VAL   A CA  1 
ATOM   1610 C  C   . VAL   A 1 215 ? -25.948 24.699  -8.465  1.00 40.06  ? 345 VAL   A C   1 
ATOM   1611 O  O   . VAL   A 1 215 ? -25.784 24.210  -7.339  1.00 38.18  ? 345 VAL   A O   1 
ATOM   1612 C  CB  . VAL   A 1 215 ? -24.722 23.787  -10.483 1.00 40.01  ? 345 VAL   A CB  1 
ATOM   1613 C  CG1 . VAL   A 1 215 ? -23.555 23.495  -9.542  1.00 35.37  ? 345 VAL   A CG1 1 
ATOM   1614 C  CG2 . VAL   A 1 215 ? -24.775 22.745  -11.581 1.00 33.96  ? 345 VAL   A CG2 1 
ATOM   1615 N  N   . THR   A 1 216 ? -26.051 26.019  -8.655  1.00 42.32  ? 346 THR   A N   1 
ATOM   1616 C  CA  . THR   A 1 216 ? -26.081 26.933  -7.514  1.00 42.93  ? 346 THR   A CA  1 
ATOM   1617 C  C   . THR   A 1 216 ? -27.192 26.546  -6.546  1.00 44.56  ? 346 THR   A C   1 
ATOM   1618 O  O   . THR   A 1 216 ? -26.997 26.530  -5.319  1.00 46.52  ? 346 THR   A O   1 
ATOM   1619 C  CB  . THR   A 1 216 ? -26.301 28.374  -7.981  1.00 42.22  ? 346 THR   A CB  1 
ATOM   1620 O  OG1 . THR   A 1 216 ? -27.499 28.435  -8.756  1.00 47.24  ? 346 THR   A OG1 1 
ATOM   1621 C  CG2 . THR   A 1 216 ? -25.173 28.849  -8.854  1.00 37.78  ? 346 THR   A CG2 1 
ATOM   1622 N  N   . GLU   A 1 217 ? -28.373 26.235  -7.093  1.00 46.16  ? 347 GLU   A N   1 
ATOM   1623 C  CA  . GLU   A 1 217 ? -29.507 25.889  -6.250  1.00 46.65  ? 347 GLU   A CA  1 
ATOM   1624 C  C   . GLU   A 1 217 ? -29.332 24.530  -5.580  1.00 47.42  ? 347 GLU   A C   1 
ATOM   1625 O  O   . GLU   A 1 217 ? -29.845 24.305  -4.468  1.00 47.38  ? 347 GLU   A O   1 
ATOM   1626 C  CB  . GLU   A 1 217 ? -30.776 25.930  -7.076  1.00 49.17  ? 347 GLU   A CB  1 
ATOM   1627 C  CG  . GLU   A 1 217 ? -31.047 27.275  -7.698  1.00 49.78  ? 347 GLU   A CG  1 
ATOM   1628 C  CD  . GLU   A 1 217 ? -31.783 28.180  -6.733  1.00 69.19  ? 347 GLU   A CD  1 
ATOM   1629 O  OE1 . GLU   A 1 217 ? -33.031 28.065  -6.628  1.00 70.19  ? 347 GLU   A OE1 1 
ATOM   1630 O  OE2 . GLU   A 1 217 ? -31.111 28.947  -6.026  1.00 72.18  ? 347 GLU   A OE2 1 
ATOM   1631 N  N   . LYS   A 1 218 ? -28.645 23.593  -6.250  1.00 43.25  ? 348 LYS   A N   1 
ATOM   1632 C  CA  . LYS   A 1 218 ? -28.345 22.347  -5.557  1.00 43.90  ? 348 LYS   A CA  1 
ATOM   1633 C  C   . LYS   A 1 218 ? -27.342 22.582  -4.435  1.00 42.14  ? 348 LYS   A C   1 
ATOM   1634 O  O   . LYS   A 1 218 ? -27.487 22.035  -3.332  1.00 42.78  ? 348 LYS   A O   1 
ATOM   1635 C  CB  . LYS   A 1 218 ? -27.824 21.311  -6.538  1.00 43.24  ? 348 LYS   A CB  1 
ATOM   1636 C  CG  . LYS   A 1 218 ? -27.802 19.904  -6.006  1.00 39.74  ? 348 LYS   A CG  1 
ATOM   1637 C  CD  . LYS   A 1 218 ? -29.022 19.688  -5.114  1.00 46.91  ? 348 LYS   A CD  1 
ATOM   1638 C  CE  . LYS   A 1 218 ? -30.164 18.997  -5.853  1.00 48.15  ? 348 LYS   A CE  1 
ATOM   1639 N  NZ  . LYS   A 1 218 ? -30.997 18.133  -4.962  1.00 46.83  ? 348 LYS   A NZ  1 
ATOM   1640 N  N   . LEU   A 1 219 ? -26.301 23.367  -4.719  1.00 40.85  ? 349 LEU   A N   1 
ATOM   1641 C  CA  . LEU   A 1 219 ? -25.290 23.674  -3.714  1.00 41.10  ? 349 LEU   A CA  1 
ATOM   1642 C  C   . LEU   A 1 219 ? -25.904 24.382  -2.512  1.00 45.67  ? 349 LEU   A C   1 
ATOM   1643 O  O   . LEU   A 1 219 ? -25.482 24.161  -1.369  1.00 46.57  ? 349 LEU   A O   1 
ATOM   1644 C  CB  . LEU   A 1 219 ? -24.190 24.535  -4.336  1.00 42.70  ? 349 LEU   A CB  1 
ATOM   1645 C  CG  . LEU   A 1 219 ? -23.211 23.785  -5.243  1.00 38.20  ? 349 LEU   A CG  1 
ATOM   1646 C  CD1 . LEU   A 1 219 ? -22.188 24.737  -5.838  1.00 34.57  ? 349 LEU   A CD1 1 
ATOM   1647 C  CD2 . LEU   A 1 219 ? -22.528 22.666  -4.481  1.00 37.40  ? 349 LEU   A CD2 1 
ATOM   1648 N  N   . LYS   A 1 220 ? -26.896 25.248  -2.756  1.00 42.15  ? 350 LYS   A N   1 
ATOM   1649 C  CA  . LYS   A 1 220 ? -27.598 25.939  -1.676  1.00 45.10  ? 350 LYS   A CA  1 
ATOM   1650 C  C   . LYS   A 1 220 ? -28.166 24.956  -0.664  1.00 44.85  ? 350 LYS   A C   1 
ATOM   1651 O  O   . LYS   A 1 220 ? -28.075 25.177  0.551   1.00 50.23  ? 350 LYS   A O   1 
ATOM   1652 C  CB  . LYS   A 1 220 ? -28.719 26.802  -2.261  1.00 47.76  ? 350 LYS   A CB  1 
ATOM   1653 C  CG  . LYS   A 1 220 ? -28.351 28.259  -2.480  1.00 48.30  ? 350 LYS   A CG  1 
ATOM   1654 C  CD  . LYS   A 1 220 ? -29.496 29.002  -3.154  1.00 51.11  ? 350 LYS   A CD  1 
ATOM   1655 C  CE  . LYS   A 1 220 ? -30.048 30.116  -2.284  1.00 56.98  ? 350 LYS   A CE  1 
ATOM   1656 N  NZ  . LYS   A 1 220 ? -28.973 30.842  -1.561  1.00 58.71  ? 350 LYS   A NZ  1 
ATOM   1657 N  N   . GLU   A 1 221 ? -28.755 23.861  -1.154  1.00 41.53  ? 351 GLU   A N   1 
ATOM   1658 C  CA  . GLU   A 1 221 ? -29.341 22.858  -0.272  1.00 44.19  ? 351 GLU   A CA  1 
ATOM   1659 C  C   . GLU   A 1 221 ? -28.301 22.275  0.677   1.00 47.34  ? 351 GLU   A C   1 
ATOM   1660 O  O   . GLU   A 1 221 ? -28.623 21.895  1.810   1.00 44.56  ? 351 GLU   A O   1 
ATOM   1661 C  CB  . GLU   A 1 221 ? -29.983 21.750  -1.103  1.00 46.28  ? 351 GLU   A CB  1 
ATOM   1662 C  CG  . GLU   A 1 221 ? -31.015 22.256  -2.104  1.00 49.57  ? 351 GLU   A CG  1 
ATOM   1663 C  CD  . GLU   A 1 221 ? -31.596 21.143  -2.953  1.00 55.71  ? 351 GLU   A CD  1 
ATOM   1664 O  OE1 . GLU   A 1 221 ? -31.483 19.969  -2.540  1.00 56.61  ? 351 GLU   A OE1 1 
ATOM   1665 O  OE2 . GLU   A 1 221 ? -32.162 21.430  -4.033  1.00 60.66  ? 351 GLU   A OE2 1 
ATOM   1666 N  N   . HIS   A 1 222 ? -27.051 22.190  0.230   1.00 43.48  ? 352 HIS   A N   1 
ATOM   1667 C  CA  . HIS   A 1 222 ? -25.971 21.661  1.049   1.00 41.66  ? 352 HIS   A CA  1 
ATOM   1668 C  C   . HIS   A 1 222 ? -25.262 22.707  1.890   1.00 44.17  ? 352 HIS   A C   1 
ATOM   1669 O  O   . HIS   A 1 222 ? -24.579 22.340  2.852   1.00 47.28  ? 352 HIS   A O   1 
ATOM   1670 C  CB  . HIS   A 1 222 ? -24.946 20.945  0.170   1.00 42.38  ? 352 HIS   A CB  1 
ATOM   1671 C  CG  . HIS   A 1 222 ? -25.505 19.793  -0.602  1.00 40.17  ? 352 HIS   A CG  1 
ATOM   1672 N  ND1 . HIS   A 1 222 ? -25.460 18.502  -0.127  1.00 37.97  ? 352 HIS   A ND1 1 
ATOM   1673 C  CD2 . HIS   A 1 222 ? -26.102 19.725  -1.814  1.00 38.15  ? 352 HIS   A CD2 1 
ATOM   1674 C  CE1 . HIS   A 1 222 ? -26.023 17.690  -1.003  1.00 43.03  ? 352 HIS   A CE1 1 
ATOM   1675 N  NE2 . HIS   A 1 222 ? -26.419 18.407  -2.039  1.00 39.25  ? 352 HIS   A NE2 1 
ATOM   1676 N  N   . PHE   A 1 223 ? -25.408 23.986  1.569   1.00 42.06  ? 353 PHE   A N   1 
ATOM   1677 C  CA  . PHE   A 1 223 ? -24.685 25.009  2.308   1.00 42.64  ? 353 PHE   A CA  1 
ATOM   1678 C  C   . PHE   A 1 223 ? -25.605 26.065  2.894   1.00 47.08  ? 353 PHE   A C   1 
ATOM   1679 O  O   . PHE   A 1 223 ? -25.367 27.269  2.752   1.00 48.20  ? 353 PHE   A O   1 
ATOM   1680 C  CB  . PHE   A 1 223 ? -23.609 25.624  1.418   1.00 39.00  ? 353 PHE   A CB  1 
ATOM   1681 C  CG  . PHE   A 1 223 ? -22.493 24.671  1.109   1.00 44.35  ? 353 PHE   A CG  1 
ATOM   1682 C  CD1 . PHE   A 1 223 ? -21.485 24.462  2.033   1.00 40.82  ? 353 PHE   A CD1 1 
ATOM   1683 C  CD2 . PHE   A 1 223 ? -22.469 23.958  -0.076  1.00 37.49  ? 353 PHE   A CD2 1 
ATOM   1684 C  CE1 . PHE   A 1 223 ? -20.466 23.577  1.774   1.00 38.49  ? 353 PHE   A CE1 1 
ATOM   1685 C  CE2 . PHE   A 1 223 ? -21.449 23.075  -0.339  1.00 40.61  ? 353 PHE   A CE2 1 
ATOM   1686 C  CZ  . PHE   A 1 223 ? -20.447 22.884  0.586   1.00 41.23  ? 353 PHE   A CZ  1 
ATOM   1687 N  N   . ASN   A 1 224 ? -26.649 25.598  3.574   1.00 48.12  ? 354 ASN   A N   1 
ATOM   1688 C  CA  . ASN   A 1 224 ? -27.439 26.426  4.481   1.00 50.04  ? 354 ASN   A CA  1 
ATOM   1689 C  C   . ASN   A 1 224 ? -28.009 27.647  3.770   1.00 50.83  ? 354 ASN   A C   1 
ATOM   1690 O  O   . ASN   A 1 224 ? -28.189 28.707  4.372   1.00 54.03  ? 354 ASN   A O   1 
ATOM   1691 C  CB  . ASN   A 1 224 ? -26.612 26.854  5.697   1.00 53.48  ? 354 ASN   A CB  1 
ATOM   1692 C  CG  . ASN   A 1 224 ? -26.463 25.747  6.723   1.00 62.18  ? 354 ASN   A CG  1 
ATOM   1693 O  OD1 . ASN   A 1 224 ? -27.441 25.096  7.093   1.00 71.16  ? 354 ASN   A OD1 1 
ATOM   1694 N  ND2 . ASN   A 1 224 ? -25.239 25.544  7.209   1.00 60.45  ? 354 ASN   A ND2 1 
ATOM   1695 N  N   . ASN   A 1 225 ? -28.279 27.507  2.470   1.00 51.77  ? 355 ASN   A N   1 
ATOM   1696 C  CA  . ASN   A 1 225 ? -28.874 28.589  1.683   1.00 57.33  ? 355 ASN   A CA  1 
ATOM   1697 C  C   . ASN   A 1 225 ? -27.971 29.821  1.678   1.00 52.07  ? 355 ASN   A C   1 
ATOM   1698 O  O   . ASN   A 1 225 ? -28.447 30.960  1.620   1.00 52.94  ? 355 ASN   A O   1 
ATOM   1699 C  CB  . ASN   A 1 225 ? -30.275 28.915  2.215   1.00 60.81  ? 355 ASN   A CB  1 
ATOM   1700 C  CG  . ASN   A 1 225 ? -31.350 28.783  1.143   1.00 64.70  ? 355 ASN   A CG  1 
ATOM   1701 O  OD1 . ASN   A 1 225 ? -31.569 27.695  0.617   1.00 58.99  ? 355 ASN   A OD1 1 
ATOM   1702 N  ND2 . ASN   A 1 225 ? -32.125 29.859  0.933   1.00 72.37  ? 355 ASN   A ND2 1 
ATOM   1703 N  N   . LYS   A 1 226 ? -26.666 29.582  1.798   1.00 49.69  ? 357 LYS   A N   1 
ATOM   1704 C  CA  . LYS   A 1 226 ? -25.655 30.614  1.679   1.00 44.65  ? 357 LYS   A CA  1 
ATOM   1705 C  C   . LYS   A 1 226 ? -25.547 31.053  0.223   1.00 44.66  ? 357 LYS   A C   1 
ATOM   1706 O  O   . LYS   A 1 226 ? -25.891 30.314  -0.706  1.00 41.58  ? 357 LYS   A O   1 
ATOM   1707 C  CB  . LYS   A 1 226 ? -24.306 30.095  2.188   1.00 46.31  ? 357 LYS   A CB  1 
ATOM   1708 C  CG  . LYS   A 1 226 ? -24.137 30.219  3.696   1.00 47.47  ? 357 LYS   A CG  1 
ATOM   1709 C  CD  . LYS   A 1 226 ? -22.712 29.912  4.158   1.00 46.01  ? 357 LYS   A CD  1 
ATOM   1710 C  CE  . LYS   A 1 226 ? -21.792 31.112  4.035   1.00 42.20  ? 357 LYS   A CE  1 
ATOM   1711 N  NZ  . LYS   A 1 226 ? -20.455 30.857  4.652   1.00 46.23  ? 357 LYS   A NZ  1 
ATOM   1712 N  N   . THR   A 1 227 ? -25.093 32.286  0.030   1.00 43.71  ? 358 THR   A N   1 
ATOM   1713 C  CA  . THR   A 1 227 ? -24.880 32.786  -1.320  1.00 44.81  ? 358 THR   A CA  1 
ATOM   1714 C  C   . THR   A 1 227 ? -23.783 31.979  -1.996  1.00 43.64  ? 358 THR   A C   1 
ATOM   1715 O  O   . THR   A 1 227 ? -22.665 31.881  -1.482  1.00 45.29  ? 358 THR   A O   1 
ATOM   1716 C  CB  . THR   A 1 227 ? -24.508 34.266  -1.294  1.00 45.01  ? 358 THR   A CB  1 
ATOM   1717 O  OG1 . THR   A 1 227 ? -25.516 35.011  -0.602  1.00 42.13  ? 358 THR   A OG1 1 
ATOM   1718 C  CG2 . THR   A 1 227 ? -24.375 34.798  -2.707  1.00 41.41  ? 358 THR   A CG2 1 
ATOM   1719 N  N   . ILE   A 1 228 ? -24.112 31.390  -3.141  1.00 42.01  ? 359 ILE   A N   1 
ATOM   1720 C  CA  . ILE   A 1 228 ? -23.188 30.551  -3.891  1.00 42.73  ? 359 ILE   A CA  1 
ATOM   1721 C  C   . ILE   A 1 228 ? -22.537 31.403  -4.972  1.00 41.92  ? 359 ILE   A C   1 
ATOM   1722 O  O   . ILE   A 1 228 ? -23.218 31.896  -5.878  1.00 44.27  ? 359 ILE   A O   1 
ATOM   1723 C  CB  . ILE   A 1 228 ? -23.905 29.338  -4.506  1.00 42.85  ? 359 ILE   A CB  1 
ATOM   1724 C  CG1 . ILE   A 1 228 ? -24.481 28.426  -3.417  1.00 45.91  ? 359 ILE   A CG1 1 
ATOM   1725 C  CG2 . ILE   A 1 228 ? -22.954 28.561  -5.405  1.00 39.15  ? 359 ILE   A CG2 1 
ATOM   1726 C  CD1 . ILE   A 1 228 ? -23.539 28.154  -2.260  1.00 45.09  ? 359 ILE   A CD1 1 
ATOM   1727 N  N   . ILE   A 1 229 ? -21.218 31.565  -4.892  1.00 40.60  ? 360 ILE   A N   1 
ATOM   1728 C  CA  . ILE   A 1 229 ? -20.459 32.333  -5.871  1.00 40.66  ? 360 ILE   A CA  1 
ATOM   1729 C  C   . ILE   A 1 229 ? -19.518 31.392  -6.611  1.00 41.65  ? 360 ILE   A C   1 
ATOM   1730 O  O   . ILE   A 1 229 ? -18.924 30.492  -6.009  1.00 35.81  ? 360 ILE   A O   1 
ATOM   1731 C  CB  . ILE   A 1 229 ? -19.676 33.486  -5.206  1.00 44.02  ? 360 ILE   A CB  1 
ATOM   1732 C  CG1 . ILE   A 1 229 ? -20.613 34.652  -4.893  1.00 43.20  ? 360 ILE   A CG1 1 
ATOM   1733 C  CG2 . ILE   A 1 229 ? -18.533 33.965  -6.091  1.00 43.37  ? 360 ILE   A CG2 1 
ATOM   1734 C  CD1 . ILE   A 1 229 ? -20.379 35.275  -3.543  1.00 41.94  ? 360 ILE   A CD1 1 
ATOM   1735 N  N   . PHE   A 1 230 ? -19.405 31.582  -7.922  1.00 42.92  ? 361 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A 1 230 ? -18.440 30.863  -8.738  1.00 41.92  ? 361 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A 1 230 ? -17.329 31.819  -9.138  1.00 42.98  ? 361 PHE   A C   1 
ATOM   1738 O  O   . PHE   A 1 230 ? -17.583 32.995  -9.413  1.00 42.50  ? 361 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A 1 230 ? -19.101 30.278  -9.988  1.00 39.52  ? 361 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A 1 230 ? -19.926 29.063  -9.712  1.00 41.29  ? 361 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A 1 230 ? -19.350 27.808  -9.684  1.00 31.88  ? 361 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A 1 230 ? -21.278 29.178  -9.457  1.00 41.37  ? 361 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A 1 230 ? -20.113 26.688  -9.422  1.00 41.33  ? 361 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A 1 230 ? -22.035 28.064  -9.193  1.00 40.00  ? 361 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A 1 230 ? -21.458 26.818  -9.175  1.00 38.91  ? 361 PHE   A CZ  1 
ATOM   1746 N  N   . GLN   A 1 231 ? -16.103 31.322  -9.162  1.00 41.47  ? 362 GLN   A N   1 
ATOM   1747 C  CA  . GLN   A 1 231 ? -14.963 32.134  -9.550  1.00 39.07  ? 362 GLN   A CA  1 
ATOM   1748 C  C   . GLN   A 1 231 ? -13.984 31.252  -10.314 1.00 40.89  ? 362 GLN   A C   1 
ATOM   1749 O  O   . GLN   A 1 231 ? -14.029 30.026  -10.197 1.00 36.39  ? 362 GLN   A O   1 
ATOM   1750 C  CB  . GLN   A 1 231 ? -14.280 32.756  -8.326  1.00 39.67  ? 362 GLN   A CB  1 
ATOM   1751 C  CG  . GLN   A 1 231 ? -14.991 33.996  -7.805  1.00 46.58  ? 362 GLN   A CG  1 
ATOM   1752 C  CD  . GLN   A 1 231 ? -14.974 35.143  -8.800  1.00 44.98  ? 362 GLN   A CD  1 
ATOM   1753 O  OE1 . GLN   A 1 231 ? -13.951 35.807  -8.981  1.00 44.86  ? 362 GLN   A OE1 1 
ATOM   1754 N  NE2 . GLN   A 1 231 ? -16.112 35.385  -9.447  1.00 46.65  ? 362 GLN   A NE2 1 
ATOM   1755 N  N   . PRO   A 1 232 ? -13.110 31.853  -11.117 1.00 37.25  ? 363 PRO   A N   1 
ATOM   1756 C  CA  . PRO   A 1 232 ? -12.065 31.065  -11.779 1.00 36.99  ? 363 PRO   A CA  1 
ATOM   1757 C  C   . PRO   A 1 232 ? -11.110 30.470  -10.761 1.00 38.81  ? 363 PRO   A C   1 
ATOM   1758 O  O   . PRO   A 1 232 ? -11.050 30.940  -9.615  1.00 38.98  ? 363 PRO   A O   1 
ATOM   1759 C  CB  . PRO   A 1 232 ? -11.360 32.097  -12.676 1.00 39.90  ? 363 PRO   A CB  1 
ATOM   1760 C  CG  . PRO   A 1 232 ? -12.403 33.183  -12.878 1.00 36.81  ? 363 PRO   A CG  1 
ATOM   1761 C  CD  . PRO   A 1 232 ? -13.094 33.261  -11.555 1.00 40.89  ? 363 PRO   A CD  1 
ATOM   1762 N  N   . PRO   A 1 233 ? -10.361 29.426  -11.129 1.00 36.37  ? 364 PRO   A N   1 
ATOM   1763 C  CA  . PRO   A 1 233 ? -9.395  28.853  -10.187 1.00 38.44  ? 364 PRO   A CA  1 
ATOM   1764 C  C   . PRO   A 1 233 ? -8.401  29.904  -9.725  1.00 46.10  ? 364 PRO   A C   1 
ATOM   1765 O  O   . PRO   A 1 233 ? -7.980  30.767  -10.499 1.00 45.37  ? 364 PRO   A O   1 
ATOM   1766 C  CB  . PRO   A 1 233 ? -8.726  27.749  -11.012 1.00 39.20  ? 364 PRO   A CB  1 
ATOM   1767 C  CG  . PRO   A 1 233 ? -9.782  27.392  -12.011 1.00 36.18  ? 364 PRO   A CG  1 
ATOM   1768 C  CD  . PRO   A 1 233 ? -10.303 28.725  -12.423 1.00 38.83  ? 364 PRO   A CD  1 
ATOM   1769 N  N   . SER   A 1 234 ? -8.051  29.838  -8.440  1.00 37.77  ? 365 SER   A N   1 
ATOM   1770 C  CA  . SER   A 1 234 ? -7.121  30.795  -7.841  1.00 47.81  ? 365 SER   A CA  1 
ATOM   1771 C  C   . SER   A 1 234 ? -5.726  30.173  -7.828  1.00 48.24  ? 365 SER   A C   1 
ATOM   1772 O  O   . SER   A 1 234 ? -5.249  29.636  -6.826  1.00 55.93  ? 365 SER   A O   1 
ATOM   1773 C  CB  . SER   A 1 234 ? -7.588  31.208  -6.448  1.00 46.05  ? 365 SER   A CB  1 
ATOM   1774 O  OG  . SER   A 1 234 ? -7.674  30.095  -5.578  1.00 50.54  ? 365 SER   A OG  1 
ATOM   1775 N  N   . GLY   A 1 235 ? -5.058  30.261  -8.973  1.00 49.88  ? 366 GLY   A N   1 
ATOM   1776 C  CA  . GLY   A 1 235 ? -3.699  29.781  -9.099  1.00 45.98  ? 366 GLY   A CA  1 
ATOM   1777 C  C   . GLY   A 1 235 ? -3.627  28.293  -9.388  1.00 39.35  ? 366 GLY   A C   1 
ATOM   1778 O  O   . GLY   A 1 235 ? -4.569  27.535  -9.176  1.00 47.66  ? 366 GLY   A O   1 
ATOM   1779 N  N   . GLY   A 1 236 ? -2.470  27.880  -9.879  1.00 36.79  ? 367 GLY   A N   1 
ATOM   1780 C  CA  . GLY   A 1 236 ? -2.206  26.502  -10.214 1.00 40.66  ? 367 GLY   A CA  1 
ATOM   1781 C  C   . GLY   A 1 236 ? -1.745  26.373  -11.644 1.00 38.57  ? 367 GLY   A C   1 
ATOM   1782 O  O   . GLY   A 1 236 ? -1.608  27.350  -12.376 1.00 38.46  ? 367 GLY   A O   1 
ATOM   1783 N  N   . ASP   A 1 237 ? -1.503  25.129  -12.041 1.00 37.63  ? 368 ASP   A N   1 
ATOM   1784 C  CA  . ASP   A 1 237 ? -1.010  24.853  -13.378 1.00 35.52  ? 368 ASP   A CA  1 
ATOM   1785 C  C   . ASP   A 1 237 ? -2.125  25.023  -14.406 1.00 31.08  ? 368 ASP   A C   1 
ATOM   1786 O  O   . ASP   A 1 237 ? -3.318  24.955  -14.092 1.00 30.67  ? 368 ASP   A O   1 
ATOM   1787 C  CB  . ASP   A 1 237 ? -0.425  23.443  -13.451 1.00 35.25  ? 368 ASP   A CB  1 
ATOM   1788 C  CG  . ASP   A 1 237 ? 0.710   23.240  -12.474 1.00 43.33  ? 368 ASP   A CG  1 
ATOM   1789 O  OD1 . ASP   A 1 237 ? 1.827   23.716  -12.769 1.00 45.86  ? 368 ASP   A OD1 1 
ATOM   1790 O  OD2 . ASP   A 1 237 ? 0.496   22.616  -11.410 1.00 44.67  ? 368 ASP   A OD2 1 
ATOM   1791 N  N   . LEU   A 1 238 ? -1.711  25.263  -15.653 1.00 28.42  ? 369 LEU   A N   1 
ATOM   1792 C  CA  . LEU   A 1 238 ? -2.659  25.518  -16.736 1.00 29.12  ? 369 LEU   A CA  1 
ATOM   1793 C  C   . LEU   A 1 238 ? -3.635  24.365  -16.929 1.00 31.23  ? 369 LEU   A C   1 
ATOM   1794 O  O   . LEU   A 1 238 ? -4.768  24.579  -17.374 1.00 30.62  ? 369 LEU   A O   1 
ATOM   1795 C  CB  . LEU   A 1 238 ? -1.897  25.778  -18.034 1.00 26.47  ? 369 LEU   A CB  1 
ATOM   1796 C  CG  . LEU   A 1 238 ? -1.633  27.233  -18.422 1.00 37.34  ? 369 LEU   A CG  1 
ATOM   1797 C  CD1 . LEU   A 1 238 ? -1.142  28.045  -17.231 1.00 38.66  ? 369 LEU   A CD1 1 
ATOM   1798 C  CD2 . LEU   A 1 238 ? -0.624  27.283  -19.551 1.00 35.75  ? 369 LEU   A CD2 1 
ATOM   1799 N  N   . GLU   A 1 239 ? -3.212  23.139  -16.619 1.00 28.16  ? 370 GLU   A N   1 
ATOM   1800 C  CA  . GLU   A 1 239 ? -4.093  21.994  -16.804 1.00 30.44  ? 370 GLU   A CA  1 
ATOM   1801 C  C   . GLU   A 1 239 ? -5.341  22.102  -15.939 1.00 31.56  ? 370 GLU   A C   1 
ATOM   1802 O  O   . GLU   A 1 239 ? -6.416  21.654  -16.347 1.00 32.33  ? 370 GLU   A O   1 
ATOM   1803 C  CB  . GLU   A 1 239 ? -3.337  20.701  -16.509 1.00 29.19  ? 370 GLU   A CB  1 
ATOM   1804 C  CG  . GLU   A 1 239 ? -2.287  20.347  -17.552 1.00 31.94  ? 370 GLU   A CG  1 
ATOM   1805 C  CD  . GLU   A 1 239 ? -1.033  21.206  -17.462 1.00 31.63  ? 370 GLU   A CD  1 
ATOM   1806 O  OE1 . GLU   A 1 239 ? -0.738  21.736  -16.366 1.00 28.97  ? 370 GLU   A OE1 1 
ATOM   1807 O  OE2 . GLU   A 1 239 ? -0.337  21.356  -18.493 1.00 30.08  ? 370 GLU   A OE2 1 
ATOM   1808 N  N   . ILE   A 1 240 ? -5.232  22.723  -14.767 1.00 30.85  ? 371 ILE   A N   1 
ATOM   1809 C  CA  . ILE   A 1 240 ? -6.365  22.855  -13.860 1.00 32.95  ? 371 ILE   A CA  1 
ATOM   1810 C  C   . ILE   A 1 240 ? -6.976  24.254  -13.879 1.00 32.91  ? 371 ILE   A C   1 
ATOM   1811 O  O   . ILE   A 1 240 ? -8.187  24.383  -13.633 1.00 36.01  ? 371 ILE   A O   1 
ATOM   1812 C  CB  . ILE   A 1 240 ? -5.975  22.452  -12.421 1.00 35.59  ? 371 ILE   A CB  1 
ATOM   1813 C  CG1 . ILE   A 1 240 ? -5.344  21.056  -12.424 1.00 37.73  ? 371 ILE   A CG1 1 
ATOM   1814 C  CG2 . ILE   A 1 240 ? -7.188  22.445  -11.500 1.00 41.48  ? 371 ILE   A CG2 1 
ATOM   1815 C  CD1 . ILE   A 1 240 ? -4.245  20.859  -11.405 1.00 41.17  ? 371 ILE   A CD1 1 
ATOM   1816 N  N   . THR   A 1 241 ? -6.201  25.299  -14.185 1.00 26.98  ? 372 THR   A N   1 
ATOM   1817 C  CA  . THR   A 1 241 ? -6.793  26.627  -14.314 1.00 30.98  ? 372 THR   A CA  1 
ATOM   1818 C  C   . THR   A 1 241 ? -7.577  26.771  -15.611 1.00 32.71  ? 372 THR   A C   1 
ATOM   1819 O  O   . THR   A 1 241 ? -8.487  27.605  -15.695 1.00 33.16  ? 372 THR   A O   1 
ATOM   1820 C  CB  . THR   A 1 241 ? -5.719  27.713  -14.238 1.00 35.11  ? 372 THR   A CB  1 
ATOM   1821 O  OG1 . THR   A 1 241 ? -4.775  27.535  -15.300 1.00 26.28  ? 372 THR   A OG1 1 
ATOM   1822 C  CG2 . THR   A 1 241 ? -4.980  27.632  -12.914 1.00 36.84  ? 372 THR   A CG2 1 
ATOM   1823 N  N   . MET   A 1 242 ? -7.234  25.984  -16.623 1.00 27.41  ? 373 MET   A N   1 
ATOM   1824 C  CA  . MET   A 1 242 ? -8.010  25.852  -17.846 1.00 29.16  ? 373 MET   A CA  1 
ATOM   1825 C  C   . MET   A 1 242 ? -8.805  24.555  -17.794 1.00 30.44  ? 373 MET   A C   1 
ATOM   1826 O  O   . MET   A 1 242 ? -8.549  23.675  -16.968 1.00 30.28  ? 373 MET   A O   1 
ATOM   1827 C  CB  . MET   A 1 242 ? -7.092  25.854  -19.075 1.00 29.17  ? 373 MET   A CB  1 
ATOM   1828 C  CG  . MET   A 1 242 ? -6.120  27.009  -19.122 1.00 35.88  ? 373 MET   A CG  1 
ATOM   1829 S  SD  . MET   A 1 242 ? -6.789  28.444  -19.968 1.00 47.25  ? 373 MET   A SD  1 
ATOM   1830 C  CE  . MET   A 1 242 ? -5.270  29.300  -20.388 1.00 47.76  ? 373 MET   A CE  1 
ATOM   1831 N  N   . HIS   A 1 243 ? -9.787  24.442  -18.683 1.00 29.31  ? 374 HIS   A N   1 
ATOM   1832 C  CA  . HIS   A 1 243 ? -10.457 23.167  -18.898 1.00 28.53  ? 374 HIS   A CA  1 
ATOM   1833 C  C   . HIS   A 1 243 ? -9.610  22.405  -19.904 1.00 31.42  ? 374 HIS   A C   1 
ATOM   1834 O  O   . HIS   A 1 243 ? -9.555  22.773  -21.081 1.00 27.08  ? 374 HIS   A O   1 
ATOM   1835 C  CB  . HIS   A 1 243 ? -11.886 23.364  -19.396 1.00 25.46  ? 374 HIS   A CB  1 
ATOM   1836 C  CG  . HIS   A 1 243 ? -12.472 22.165  -20.076 1.00 27.17  ? 374 HIS   A CG  1 
ATOM   1837 N  ND1 . HIS   A 1 243 ? -12.443 20.904  -19.521 1.00 24.23  ? 374 HIS   A ND1 1 
ATOM   1838 C  CD2 . HIS   A 1 243 ? -13.119 22.038  -21.258 1.00 28.23  ? 374 HIS   A CD2 1 
ATOM   1839 C  CE1 . HIS   A 1 243 ? -13.036 20.051  -20.338 1.00 26.30  ? 374 HIS   A CE1 1 
ATOM   1840 N  NE2 . HIS   A 1 243 ? -13.459 20.715  -21.398 1.00 24.34  ? 374 HIS   A NE2 1 
ATOM   1841 N  N   . SER   A 1 244 ? -8.907  21.384  -19.429 1.00 25.69  ? 375 SER   A N   1 
ATOM   1842 C  CA  . SER   A 1 244 ? -7.973  20.624  -20.241 1.00 27.65  ? 375 SER   A CA  1 
ATOM   1843 C  C   . SER   A 1 244 ? -8.600  19.295  -20.630 1.00 26.23  ? 375 SER   A C   1 
ATOM   1844 O  O   . SER   A 1 244 ? -9.317  18.683  -19.837 1.00 26.61  ? 375 SER   A O   1 
ATOM   1845 C  CB  . SER   A 1 244 ? -6.666  20.381  -19.487 1.00 30.41  ? 375 SER   A CB  1 
ATOM   1846 O  OG  . SER   A 1 244 ? -5.902  21.572  -19.428 1.00 40.96  ? 375 SER   A OG  1 
ATOM   1847 N  N   . PHE   A 1 245 ? -8.320  18.855  -21.850 1.00 23.55  ? 376 PHE   A N   1 
ATOM   1848 C  CA  . PHE   A 1 245 ? -8.821  17.584  -22.349 1.00 30.78  ? 376 PHE   A CA  1 
ATOM   1849 C  C   . PHE   A 1 245 ? -8.007  17.227  -23.580 1.00 29.73  ? 376 PHE   A C   1 
ATOM   1850 O  O   . PHE   A 1 245 ? -7.272  18.055  -24.121 1.00 29.31  ? 376 PHE   A O   1 
ATOM   1851 C  CB  . PHE   A 1 245 ? -10.316 17.652  -22.673 1.00 27.06  ? 376 PHE   A CB  1 
ATOM   1852 C  CG  . PHE   A 1 245 ? -10.686 18.752  -23.630 1.00 28.90  ? 376 PHE   A CG  1 
ATOM   1853 C  CD1 . PHE   A 1 245 ? -10.881 20.045  -23.180 1.00 29.17  ? 376 PHE   A CD1 1 
ATOM   1854 C  CD2 . PHE   A 1 245 ? -10.868 18.486  -24.979 1.00 31.27  ? 376 PHE   A CD2 1 
ATOM   1855 C  CE1 . PHE   A 1 245 ? -11.227 21.054  -24.053 1.00 29.54  ? 376 PHE   A CE1 1 
ATOM   1856 C  CE2 . PHE   A 1 245 ? -11.222 19.496  -25.859 1.00 31.72  ? 376 PHE   A CE2 1 
ATOM   1857 C  CZ  . PHE   A 1 245 ? -11.406 20.779  -25.391 1.00 33.79  ? 376 PHE   A CZ  1 
ATOM   1858 N  N   . ASN   A 1 246 ? -8.134  15.979  -24.009 1.00 26.66  ? 377 ASN   A N   1 
ATOM   1859 C  CA  . ASN   A 1 246 ? -7.497  15.509  -25.229 1.00 28.25  ? 377 ASN   A CA  1 
ATOM   1860 C  C   . ASN   A 1 246 ? -8.556  15.320  -26.301 1.00 28.96  ? 377 ASN   A C   1 
ATOM   1861 O  O   . ASN   A 1 246 ? -9.536  14.598  -26.093 1.00 33.06  ? 377 ASN   A O   1 
ATOM   1862 C  CB  . ASN   A 1 246 ? -6.716  14.217  -24.995 1.00 30.27  ? 377 ASN   A CB  1 
ATOM   1863 C  CG  . ASN   A 1 246 ? -5.913  13.815  -26.204 1.00 29.06  ? 377 ASN   A CG  1 
ATOM   1864 O  OD1 . ASN   A 1 246 ? -6.479  13.515  -27.252 1.00 27.01  ? 377 ASN   A OD1 1 
ATOM   1865 N  ND2 . ASN   A 1 246 ? -4.590  13.867  -26.089 1.00 33.83  ? 377 ASN   A ND2 1 
ATOM   1866 N  N   . CYS   A 1 247 ? -8.350  15.973  -27.439 1.00 28.60  ? 378 CYS   A N   1 
ATOM   1867 C  CA  . CYS   A 1 247 ? -9.240  15.880  -28.583 1.00 31.44  ? 378 CYS   A CA  1 
ATOM   1868 C  C   . CYS   A 1 247 ? -8.448  15.339  -29.760 1.00 28.27  ? 378 CYS   A C   1 
ATOM   1869 O  O   . CYS   A 1 247 ? -7.544  16.013  -30.261 1.00 27.87  ? 378 CYS   A O   1 
ATOM   1870 C  CB  . CYS   A 1 247 ? -9.839  17.241  -28.927 1.00 34.28  ? 378 CYS   A CB  1 
ATOM   1871 S  SG  . CYS   A 1 247 ? -10.810 17.226  -30.431 1.00 38.49  ? 378 CYS   A SG  1 
ATOM   1872 N  N   . ARG   A 1 248 ? -8.787  14.124  -30.191 1.00 28.49  ? 379 ARG   A N   1 
ATOM   1873 C  CA  . ARG   A 1 248 ? -8.155  13.478  -31.345 1.00 26.03  ? 379 ARG   A CA  1 
ATOM   1874 C  C   . ARG   A 1 248 ? -6.644  13.375  -31.178 1.00 29.58  ? 379 ARG   A C   1 
ATOM   1875 O  O   . ARG   A 1 248 ? -5.893  13.448  -32.153 1.00 30.30  ? 379 ARG   A O   1 
ATOM   1876 C  CB  . ARG   A 1 248 ? -8.481  14.211  -32.651 1.00 32.42  ? 379 ARG   A CB  1 
ATOM   1877 C  CG  . ARG   A 1 248 ? -9.911  14.699  -32.765 1.00 38.76  ? 379 ARG   A CG  1 
ATOM   1878 C  CD  . ARG   A 1 248 ? -10.851 13.754  -33.492 1.00 39.58  ? 379 ARG   A CD  1 
ATOM   1879 N  NE  . ARG   A 1 248 ? -12.234 14.129  -33.209 1.00 43.56  ? 379 ARG   A NE  1 
ATOM   1880 C  CZ  . ARG   A 1 248 ? -13.218 13.273  -32.972 1.00 41.88  ? 379 ARG   A CZ  1 
ATOM   1881 N  NH1 . ARG   A 1 248 ? -13.013 11.966  -32.973 1.00 37.34  ? 379 ARG   A NH1 1 
ATOM   1882 N  NH2 . ARG   A 1 248 ? -14.439 13.741  -32.722 1.00 37.81  ? 379 ARG   A NH2 1 
ATOM   1883 N  N   . GLY   A 1 249 ? -6.182  13.203  -29.940 1.00 26.32  ? 380 GLY   A N   1 
ATOM   1884 C  CA  . GLY   A 1 249 ? -4.762  13.152  -29.651 1.00 31.63  ? 380 GLY   A CA  1 
ATOM   1885 C  C   . GLY   A 1 249 ? -4.145  14.470  -29.239 1.00 32.59  ? 380 GLY   A C   1 
ATOM   1886 O  O   . GLY   A 1 249 ? -3.023  14.477  -28.715 1.00 35.01  ? 380 GLY   A O   1 
ATOM   1887 N  N   . GLU   A 1 250 ? -4.843  15.581  -29.442 1.00 29.22  ? 381 GLU   A N   1 
ATOM   1888 C  CA  . GLU   A 1 250 ? -4.300  16.905  -29.183 1.00 30.31  ? 381 GLU   A CA  1 
ATOM   1889 C  C   . GLU   A 1 250 ? -4.795  17.419  -27.838 1.00 27.54  ? 381 GLU   A C   1 
ATOM   1890 O  O   . GLU   A 1 250 ? -5.974  17.276  -27.505 1.00 30.32  ? 381 GLU   A O   1 
ATOM   1891 C  CB  . GLU   A 1 250 ? -4.712  17.875  -30.291 1.00 24.58  ? 381 GLU   A CB  1 
ATOM   1892 C  CG  . GLU   A 1 250 ? -4.274  17.439  -31.673 1.00 34.78  ? 381 GLU   A CG  1 
ATOM   1893 C  CD  . GLU   A 1 250 ? -2.770  17.483  -31.855 1.00 34.10  ? 381 GLU   A CD  1 
ATOM   1894 O  OE1 . GLU   A 1 250 ? -2.086  18.219  -31.109 1.00 34.21  ? 381 GLU   A OE1 1 
ATOM   1895 O  OE2 . GLU   A 1 250 ? -2.262  16.758  -32.739 1.00 39.50  ? 381 GLU   A OE2 1 
ATOM   1896 N  N   . PHE   A 1 251 ? -3.897  18.028  -27.070 1.00 25.49  ? 382 PHE   A N   1 
ATOM   1897 C  CA  . PHE   A 1 251 ? -4.242  18.537  -25.748 1.00 26.49  ? 382 PHE   A CA  1 
ATOM   1898 C  C   . PHE   A 1 251 ? -4.790  19.952  -25.873 1.00 29.51  ? 382 PHE   A C   1 
ATOM   1899 O  O   . PHE   A 1 251 ? -4.058  20.883  -26.220 1.00 25.96  ? 382 PHE   A O   1 
ATOM   1900 C  CB  . PHE   A 1 251 ? -3.038  18.484  -24.814 1.00 27.27  ? 382 PHE   A CB  1 
ATOM   1901 C  CG  . PHE   A 1 251 ? -2.626  17.092  -24.452 1.00 31.69  ? 382 PHE   A CG  1 
ATOM   1902 C  CD1 . PHE   A 1 251 ? -3.253  16.434  -23.411 1.00 29.20  ? 382 PHE   A CD1 1 
ATOM   1903 C  CD2 . PHE   A 1 251 ? -1.631  16.435  -25.152 1.00 29.34  ? 382 PHE   A CD2 1 
ATOM   1904 C  CE1 . PHE   A 1 251 ? -2.897  15.153  -23.071 1.00 27.49  ? 382 PHE   A CE1 1 
ATOM   1905 C  CE2 . PHE   A 1 251 ? -1.270  15.145  -24.814 1.00 31.89  ? 382 PHE   A CE2 1 
ATOM   1906 C  CZ  . PHE   A 1 251 ? -1.905  14.506  -23.771 1.00 28.36  ? 382 PHE   A CZ  1 
ATOM   1907 N  N   . PHE   A 1 252 ? -6.079  20.103  -25.587 1.00 31.18  ? 383 PHE   A N   1 
ATOM   1908 C  CA  . PHE   A 1 252 ? -6.757  21.387  -25.615 1.00 27.13  ? 383 PHE   A CA  1 
ATOM   1909 C  C   . PHE   A 1 252 ? -6.750  21.975  -24.212 1.00 31.18  ? 383 PHE   A C   1 
ATOM   1910 O  O   . PHE   A 1 252 ? -6.919  21.252  -23.228 1.00 27.34  ? 383 PHE   A O   1 
ATOM   1911 C  CB  . PHE   A 1 252 ? -8.202  21.240  -26.085 1.00 28.52  ? 383 PHE   A CB  1 
ATOM   1912 C  CG  . PHE   A 1 252 ? -8.368  21.150  -27.575 1.00 32.69  ? 383 PHE   A CG  1 
ATOM   1913 C  CD1 . PHE   A 1 252 ? -7.610  20.271  -28.324 1.00 28.48  ? 383 PHE   A CD1 1 
ATOM   1914 C  CD2 . PHE   A 1 252 ? -9.302  21.941  -28.223 1.00 34.66  ? 383 PHE   A CD2 1 
ATOM   1915 C  CE1 . PHE   A 1 252 ? -7.777  20.184  -29.697 1.00 31.99  ? 383 PHE   A CE1 1 
ATOM   1916 C  CE2 . PHE   A 1 252 ? -9.471  21.865  -29.592 1.00 32.97  ? 383 PHE   A CE2 1 
ATOM   1917 C  CZ  . PHE   A 1 252 ? -8.706  20.987  -30.333 1.00 36.63  ? 383 PHE   A CZ  1 
ATOM   1918 N  N   . TYR   A 1 253 ? -6.560  23.286  -24.127 1.00 29.34  ? 384 TYR   A N   1 
ATOM   1919 C  CA  . TYR   A 1 253 ? -6.600  24.030  -22.873 1.00 29.05  ? 384 TYR   A CA  1 
ATOM   1920 C  C   . TYR   A 1 253 ? -7.539  25.205  -23.086 1.00 29.42  ? 384 TYR   A C   1 
ATOM   1921 O  O   . TYR   A 1 253 ? -7.230  26.104  -23.872 1.00 29.73  ? 384 TYR   A O   1 
ATOM   1922 C  CB  . TYR   A 1 253 ? -5.208  24.530  -22.483 1.00 31.44  ? 384 TYR   A CB  1 
ATOM   1923 C  CG  . TYR   A 1 253 ? -4.251  23.485  -21.959 1.00 30.28  ? 384 TYR   A CG  1 
ATOM   1924 C  CD1 . TYR   A 1 253 ? -3.804  22.451  -22.772 1.00 29.54  ? 384 TYR   A CD1 1 
ATOM   1925 C  CD2 . TYR   A 1 253 ? -3.717  23.588  -20.685 1.00 28.12  ? 384 TYR   A CD2 1 
ATOM   1926 C  CE1 . TYR   A 1 253 ? -2.909  21.504  -22.298 1.00 29.39  ? 384 TYR   A CE1 1 
ATOM   1927 C  CE2 . TYR   A 1 253 ? -2.814  22.663  -20.211 1.00 30.60  ? 384 TYR   A CE2 1 
ATOM   1928 C  CZ  . TYR   A 1 253 ? -2.413  21.621  -21.023 1.00 30.04  ? 384 TYR   A CZ  1 
ATOM   1929 O  OH  . TYR   A 1 253 ? -1.511  20.697  -20.556 1.00 30.56  ? 384 TYR   A OH  1 
ATOM   1930 N  N   . CYS   A 1 254 ? -8.681  25.200  -22.402 1.00 29.53  ? 385 CYS   A N   1 
ATOM   1931 C  CA  . CYS   A 1 254 ? -9.744  26.156  -22.681 1.00 28.37  ? 385 CYS   A CA  1 
ATOM   1932 C  C   . CYS   A 1 254 ? -10.043 27.016  -21.464 1.00 31.87  ? 385 CYS   A C   1 
ATOM   1933 O  O   . CYS   A 1 254 ? -10.277 26.499  -20.367 1.00 30.53  ? 385 CYS   A O   1 
ATOM   1934 C  CB  . CYS   A 1 254 ? -11.007 25.439  -23.154 1.00 31.01  ? 385 CYS   A CB  1 
ATOM   1935 S  SG  . CYS   A 1 254 ? -10.750 24.627  -24.731 1.00 34.27  ? 385 CYS   A SG  1 
ATOM   1936 N  N   . ASN   A 1 255 ? -10.042 28.328  -21.675 1.00 31.77  ? 386 ASN   A N   1 
ATOM   1937 C  CA  . ASN   A 1 255 ? -10.324 29.296  -20.623 1.00 30.62  ? 386 ASN   A CA  1 
ATOM   1938 C  C   . ASN   A 1 255 ? -11.818 29.308  -20.330 1.00 31.28  ? 386 ASN   A C   1 
ATOM   1939 O  O   . ASN   A 1 255 ? -12.622 29.642  -21.204 1.00 30.22  ? 386 ASN   A O   1 
ATOM   1940 C  CB  . ASN   A 1 255 ? -9.832  30.672  -21.061 1.00 34.94  ? 386 ASN   A CB  1 
ATOM   1941 C  CG  . ASN   A 1 255 ? -9.929  31.705  -19.969 1.00 33.45  ? 386 ASN   A CG  1 
ATOM   1942 O  OD1 . ASN   A 1 255 ? -10.872 31.713  -19.181 1.00 33.94  ? 386 ASN   A OD1 1 
ATOM   1943 N  ND2 . ASN   A 1 255 ? -8.947  32.583  -19.910 1.00 39.21  ? 386 ASN   A ND2 1 
ATOM   1944 N  N   . THR   A 1 256 ? -12.187 28.955  -19.097 1.00 27.81  ? 387 THR   A N   1 
ATOM   1945 C  CA  . THR   A 1 256 ? -13.583 28.845  -18.694 1.00 32.65  ? 387 THR   A CA  1 
ATOM   1946 C  C   . THR   A 1 256 ? -14.031 30.007  -17.814 1.00 33.64  ? 387 THR   A C   1 
ATOM   1947 O  O   . THR   A 1 256 ? -15.025 29.873  -17.084 1.00 34.72  ? 387 THR   A O   1 
ATOM   1948 C  CB  . THR   A 1 256 ? -13.824 27.517  -17.969 1.00 31.31  ? 387 THR   A CB  1 
ATOM   1949 O  OG1 . THR   A 1 256 ? -13.040 27.484  -16.772 1.00 29.38  ? 387 THR   A OG1 1 
ATOM   1950 C  CG2 . THR   A 1 256 ? -13.424 26.367  -18.845 1.00 27.14  ? 387 THR   A CG2 1 
ATOM   1951 N  N   . THR   A 1 257 ? -13.309 31.135  -17.853 1.00 32.71  ? 388 THR   A N   1 
ATOM   1952 C  CA  . THR   A 1 257 ? -13.721 32.307  -17.085 1.00 37.77  ? 388 THR   A CA  1 
ATOM   1953 C  C   . THR   A 1 257 ? -15.127 32.747  -17.477 1.00 33.88  ? 388 THR   A C   1 
ATOM   1954 O  O   . THR   A 1 257 ? -15.935 33.142  -16.620 1.00 36.35  ? 388 THR   A O   1 
ATOM   1955 C  CB  . THR   A 1 257 ? -12.730 33.446  -17.301 1.00 31.99  ? 388 THR   A CB  1 
ATOM   1956 O  OG1 . THR   A 1 257 ? -11.434 33.045  -16.853 1.00 42.08  ? 388 THR   A OG1 1 
ATOM   1957 C  CG2 . THR   A 1 257 ? -13.146 34.702  -16.524 1.00 41.11  ? 388 THR   A CG2 1 
ATOM   1958 N  N   . GLN   A 1 258 ? -15.439 32.665  -18.780 1.00 33.00  ? 389 GLN   A N   1 
ATOM   1959 C  CA  . GLN   A 1 258 ? -16.769 33.004  -19.270 1.00 37.28  ? 389 GLN   A CA  1 
ATOM   1960 C  C   . GLN   A 1 258 ? -17.844 32.055  -18.749 1.00 39.39  ? 389 GLN   A C   1 
ATOM   1961 O  O   . GLN   A 1 258 ? -19.037 32.377  -18.824 1.00 42.11  ? 389 GLN   A O   1 
ATOM   1962 C  CB  . GLN   A 1 258 ? -16.774 32.967  -20.778 1.00 40.69  ? 389 GLN   A CB  1 
ATOM   1963 C  CG  . GLN   A 1 258 ? -16.389 34.247  -21.451 1.00 45.89  ? 389 GLN   A CG  1 
ATOM   1964 C  CD  . GLN   A 1 258 ? -16.216 34.076  -22.946 1.00 45.84  ? 389 GLN   A CD  1 
ATOM   1965 O  OE1 . GLN   A 1 258 ? -15.211 33.526  -23.411 1.00 46.37  ? 389 GLN   A OE1 1 
ATOM   1966 N  NE2 . GLN   A 1 258 ? -17.205 34.524  -23.709 1.00 41.33  ? 389 GLN   A NE2 1 
ATOM   1967 N  N   . LEU   A 1 259 ? -17.460 30.856  -18.310 1.00 35.46  ? 390 LEU   A N   1 
ATOM   1968 C  CA  . LEU   A 1 259 ? -18.407 29.918  -17.725 1.00 38.48  ? 390 LEU   A CA  1 
ATOM   1969 C  C   . LEU   A 1 259 ? -18.598 30.168  -16.237 1.00 39.08  ? 390 LEU   A C   1 
ATOM   1970 O  O   . LEU   A 1 259 ? -19.730 30.161  -15.742 1.00 41.73  ? 390 LEU   A O   1 
ATOM   1971 C  CB  . LEU   A 1 259 ? -17.922 28.484  -17.939 1.00 37.34  ? 390 LEU   A CB  1 
ATOM   1972 C  CG  . LEU   A 1 259 ? -17.955 27.915  -19.351 1.00 38.08  ? 390 LEU   A CG  1 
ATOM   1973 C  CD1 . LEU   A 1 259 ? -17.520 26.461  -19.317 1.00 35.93  ? 390 LEU   A CD1 1 
ATOM   1974 C  CD2 . LEU   A 1 259 ? -19.341 28.058  -19.944 1.00 38.49  ? 390 LEU   A CD2 1 
ATOM   1975 N  N   . PHE   A 1 260 ? -17.499 30.378  -15.516 1.00 39.33  ? 391 PHE   A N   1 
ATOM   1976 C  CA  . PHE   A 1 260 ? -17.514 30.465  -14.062 1.00 36.99  ? 391 PHE   A CA  1 
ATOM   1977 C  C   . PHE   A 1 260 ? -17.509 31.896  -13.569 1.00 49.80  ? 391 PHE   A C   1 
ATOM   1978 O  O   . PHE   A 1 260 ? -16.891 32.223  -12.545 1.00 44.24  ? 391 PHE   A O   1 
ATOM   1979 C  CB  . PHE   A 1 260 ? -16.359 29.646  -13.500 1.00 42.39  ? 391 PHE   A CB  1 
ATOM   1980 C  CG  . PHE   A 1 260 ? -16.577 28.188  -13.679 1.00 38.62  ? 391 PHE   A CG  1 
ATOM   1981 C  CD1 . PHE   A 1 260 ? -17.452 27.511  -12.852 1.00 40.77  ? 391 PHE   A CD1 1 
ATOM   1982 C  CD2 . PHE   A 1 260 ? -16.030 27.525  -14.760 1.00 39.15  ? 391 PHE   A CD2 1 
ATOM   1983 C  CE1 . PHE   A 1 260 ? -17.705 26.182  -13.039 1.00 35.90  ? 391 PHE   A CE1 1 
ATOM   1984 C  CE2 . PHE   A 1 260 ? -16.283 26.195  -14.956 1.00 35.28  ? 391 PHE   A CE2 1 
ATOM   1985 C  CZ  . PHE   A 1 260 ? -17.124 25.521  -14.092 1.00 38.87  ? 391 PHE   A CZ  1 
ATOM   1986 N  N   . ASN   A 1 261 ? -18.206 32.753  -14.288 1.00 48.83  ? 392 ASN   A N   1 
ATOM   1987 C  CA  . ASN   A 1 261 ? -18.607 34.060  -13.823 1.00 57.32  ? 392 ASN   A CA  1 
ATOM   1988 C  C   . ASN   A 1 261 ? -20.064 33.977  -13.403 1.00 62.59  ? 392 ASN   A C   1 
ATOM   1989 O  O   . ASN   A 1 261 ? -20.854 33.222  -13.976 1.00 63.28  ? 392 ASN   A O   1 
ATOM   1990 C  CB  . ASN   A 1 261 ? -18.429 35.093  -14.929 1.00 52.04  ? 392 ASN   A CB  1 
ATOM   1991 C  CG  . ASN   A 1 261 ? -17.061 35.723  -14.915 1.00 54.26  ? 392 ASN   A CG  1 
ATOM   1992 O  OD1 . ASN   A 1 261 ? -16.168 35.279  -14.194 1.00 52.97  ? 392 ASN   A OD1 1 
ATOM   1993 N  ND2 . ASN   A 1 261 ? -16.875 36.751  -15.741 1.00 62.27  ? 392 ASN   A ND2 1 
ATOM   1994 N  N   . ASN   A 1 262 ? -20.407 34.736  -12.371 1.00 63.73  ? 393 ASN   A N   1 
ATOM   1995 C  CA  . ASN   A 1 262 ? -21.773 34.795  -11.882 1.00 64.46  ? 393 ASN   A CA  1 
ATOM   1996 C  C   . ASN   A 1 262 ? -22.563 35.913  -12.546 1.00 68.75  ? 393 ASN   A C   1 
ATOM   1997 O  O   . ASN   A 1 262 ? -23.606 36.321  -12.022 1.00 68.88  ? 393 ASN   A O   1 
ATOM   1998 C  CB  . ASN   A 1 262 ? -21.774 34.939  -10.359 1.00 63.05  ? 393 ASN   A CB  1 
ATOM   1999 C  CG  . ASN   A 1 262 ? -20.776 34.008  -9.685  1.00 52.77  ? 393 ASN   A CG  1 
ATOM   2000 O  OD1 . ASN   A 1 262 ? -21.145 32.950  -9.167  1.00 49.84  ? 393 ASN   A OD1 1 
ATOM   2001 N  ND2 . ASN   A 1 262 ? -19.509 34.408  -9.672  1.00 55.46  ? 393 ASN   A ND2 1 
ATOM   2002 N  N   . THR   A 1 263 ? -22.062 36.414  -13.684 1.00 69.43  ? 394 THR   A N   1 
ATOM   2003 C  CA  . THR   A 1 263 ? -22.773 37.399  -14.492 1.00 70.53  ? 394 THR   A CA  1 
ATOM   2004 C  C   . THR   A 1 263 ? -24.249 37.062  -14.597 1.00 72.30  ? 394 THR   A C   1 
ATOM   2005 O  O   . THR   A 1 263 ? -25.116 37.875  -14.270 1.00 73.18  ? 394 THR   A O   1 
ATOM   2006 C  CB  . THR   A 1 263 ? -22.168 37.434  -15.894 1.00 74.27  ? 394 THR   A CB  1 
ATOM   2007 O  OG1 . THR   A 1 263 ? -20.838 36.905  -15.855 1.00 68.75  ? 394 THR   A OG1 1 
ATOM   2008 C  CG2 . THR   A 1 263 ? -22.151 38.842  -16.453 1.00 70.00  ? 394 THR   A CG2 1 
ATOM   2009 N  N   . CYS   A 1 264 ? -24.538 35.866  -15.082 1.00 73.73  ? 395 CYS   A N   1 
ATOM   2010 C  CA  . CYS   A 1 264 ? -25.873 35.385  -15.362 1.00 71.10  ? 395 CYS   A CA  1 
ATOM   2011 C  C   . CYS   A 1 264 ? -26.170 34.201  -14.436 1.00 68.65  ? 395 CYS   A C   1 
ATOM   2012 O  O   . CYS   A 1 264 ? -27.077 33.393  -14.695 1.00 70.72  ? 395 CYS   A O   1 
ATOM   2013 C  CB  . CYS   A 1 264 ? -26.009 35.008  -16.859 1.00 72.28  ? 395 CYS   A CB  1 
ATOM   2014 S  SG  . CYS   A 1 264 ? -24.705 35.588  -18.064 1.00 90.63  ? 395 CYS   A SG  1 
ATOM   2015 N  N   . GLY   A 1 272 ? -28.645 40.404  -20.978 1.00 68.02  ? 409 GLY   A N   1 
ATOM   2016 C  CA  . GLY   A 1 272 ? -27.999 40.578  -22.274 1.00 71.66  ? 409 GLY   A CA  1 
ATOM   2017 C  C   . GLY   A 1 272 ? -26.793 39.673  -22.486 1.00 76.39  ? 409 GLY   A C   1 
ATOM   2018 O  O   . GLY   A 1 272 ? -25.807 40.032  -23.125 1.00 70.38  ? 409 GLY   A O   1 
ATOM   2019 N  N   . CYS   A 1 273 ? -26.919 38.467  -21.944 1.00 78.23  ? 410 CYS   A N   1 
ATOM   2020 C  CA  . CYS   A 1 273 ? -25.880 37.436  -21.897 1.00 75.30  ? 410 CYS   A CA  1 
ATOM   2021 C  C   . CYS   A 1 273 ? -26.568 36.072  -22.006 1.00 74.34  ? 410 CYS   A C   1 
ATOM   2022 O  O   . CYS   A 1 273 ? -27.037 35.517  -21.004 1.00 73.39  ? 410 CYS   A O   1 
ATOM   2023 C  CB  . CYS   A 1 273 ? -25.040 37.601  -20.622 1.00 78.89  ? 410 CYS   A CB  1 
ATOM   2024 S  SG  . CYS   A 1 273 ? -25.796 36.985  -19.033 1.00 102.09 ? 410 CYS   A SG  1 
ATOM   2025 N  N   . ASN   A 1 274 ? -26.646 35.536  -23.232 1.00 70.11  ? 411 ASN   A N   1 
ATOM   2026 C  CA  . ASN   A 1 274 ? -27.239 34.207  -23.378 1.00 63.27  ? 411 ASN   A CA  1 
ATOM   2027 C  C   . ASN   A 1 274 ? -27.057 33.568  -24.752 1.00 57.70  ? 411 ASN   A C   1 
ATOM   2028 O  O   . ASN   A 1 274 ? -27.634 32.509  -25.016 1.00 53.70  ? 411 ASN   A O   1 
ATOM   2029 C  CB  . ASN   A 1 274 ? -28.739 34.248  -23.066 1.00 65.72  ? 411 ASN   A CB  1 
ATOM   2030 C  CG  . ASN   A 1 274 ? -29.489 35.253  -23.901 1.00 75.08  ? 411 ASN   A CG  1 
ATOM   2031 O  OD1 . ASN   A 1 274 ? -29.135 36.425  -23.963 1.00 80.12  ? 411 ASN   A OD1 1 
ATOM   2032 N  ND2 . ASN   A 1 274 ? -30.571 34.797  -24.527 1.00 74.32  ? 411 ASN   A ND2 1 
ATOM   2033 N  N   . GLY   A 1 275 ? -26.276 34.177  -25.631 1.00 54.34  ? 412 GLY   A N   1 
ATOM   2034 C  CA  . GLY   A 1 275 ? -25.981 33.590  -26.925 1.00 46.40  ? 412 GLY   A CA  1 
ATOM   2035 C  C   . GLY   A 1 275 ? -24.954 32.480  -26.818 1.00 46.95  ? 412 GLY   A C   1 
ATOM   2036 O  O   . GLY   A 1 275 ? -24.874 31.758  -25.817 1.00 42.20  ? 412 GLY   A O   1 
ATOM   2037 N  N   . THR   A 1 276 ? -24.146 32.347  -27.863 1.00 44.17  ? 413 THR   A N   1 
ATOM   2038 C  CA  . THR   A 1 276 ? -23.089 31.348  -27.882 1.00 40.83  ? 413 THR   A CA  1 
ATOM   2039 C  C   . THR   A 1 276 ? -21.891 31.842  -27.080 1.00 43.37  ? 413 THR   A C   1 
ATOM   2040 O  O   . THR   A 1 276 ? -21.363 32.928  -27.341 1.00 44.73  ? 413 THR   A O   1 
ATOM   2041 C  CB  . THR   A 1 276 ? -22.676 31.045  -29.321 1.00 43.33  ? 413 THR   A CB  1 
ATOM   2042 O  OG1 . THR   A 1 276 ? -23.754 30.388  -30.000 1.00 43.59  ? 413 THR   A OG1 1 
ATOM   2043 C  CG2 . THR   A 1 276 ? -21.447 30.155  -29.350 1.00 42.08  ? 413 THR   A CG2 1 
ATOM   2044 N  N   . ILE   A 1 277 ? -21.475 31.051  -26.096 1.00 39.29  ? 414 ILE   A N   1 
ATOM   2045 C  CA  . ILE   A 1 277 ? -20.261 31.321  -25.335 1.00 38.25  ? 414 ILE   A CA  1 
ATOM   2046 C  C   . ILE   A 1 277 ? -19.096 30.706  -26.096 1.00 39.95  ? 414 ILE   A C   1 
ATOM   2047 O  O   . ILE   A 1 277 ? -19.069 29.492  -26.324 1.00 39.51  ? 414 ILE   A O   1 
ATOM   2048 C  CB  . ILE   A 1 277 ? -20.343 30.741  -23.915 1.00 39.23  ? 414 ILE   A CB  1 
ATOM   2049 C  CG1 . ILE   A 1 277 ? -21.465 31.384  -23.103 1.00 38.65  ? 414 ILE   A CG1 1 
ATOM   2050 C  CG2 . ILE   A 1 277 ? -19.037 30.949  -23.189 1.00 38.87  ? 414 ILE   A CG2 1 
ATOM   2051 C  CD1 . ILE   A 1 277 ? -21.674 30.725  -21.755 1.00 41.43  ? 414 ILE   A CD1 1 
ATOM   2052 N  N   . THR   A 1 278 ? -18.130 31.531  -26.483 1.00 37.42  ? 415 THR   A N   1 
ATOM   2053 C  CA  . THR   A 1 278 ? -16.949 31.060  -27.196 1.00 37.49  ? 415 THR   A CA  1 
ATOM   2054 C  C   . THR   A 1 278 ? -15.757 31.121  -26.250 1.00 40.23  ? 415 THR   A C   1 
ATOM   2055 O  O   . THR   A 1 278 ? -15.284 32.212  -25.909 1.00 39.63  ? 415 THR   A O   1 
ATOM   2056 C  CB  . THR   A 1 278 ? -16.690 31.896  -28.444 1.00 42.54  ? 415 THR   A CB  1 
ATOM   2057 O  OG1 . THR   A 1 278 ? -17.790 31.755  -29.350 1.00 41.65  ? 415 THR   A OG1 1 
ATOM   2058 C  CG2 . THR   A 1 278 ? -15.427 31.418  -29.131 1.00 38.49  ? 415 THR   A CG2 1 
ATOM   2059 N  N   . LEU   A 1 279 ? -15.274 29.952  -25.836 1.00 34.35  ? 416 LEU   A N   1 
ATOM   2060 C  CA  . LEU   A 1 279 ? -14.106 29.904  -24.968 1.00 38.03  ? 416 LEU   A CA  1 
ATOM   2061 C  C   . LEU   A 1 279 ? -12.852 29.894  -25.824 1.00 31.41  ? 416 LEU   A C   1 
ATOM   2062 O  O   . LEU   A 1 279 ? -12.753 29.074  -26.742 1.00 35.29  ? 416 LEU   A O   1 
ATOM   2063 C  CB  . LEU   A 1 279 ? -14.122 28.653  -24.104 1.00 30.63  ? 416 LEU   A CB  1 
ATOM   2064 C  CG  . LEU   A 1 279 ? -15.308 28.392  -23.176 1.00 37.87  ? 416 LEU   A CG  1 
ATOM   2065 C  CD1 . LEU   A 1 279 ? -15.159 27.006  -22.533 1.00 31.16  ? 416 LEU   A CD1 1 
ATOM   2066 C  CD2 . LEU   A 1 279 ? -15.518 29.495  -22.144 1.00 31.55  ? 416 LEU   A CD2 1 
ATOM   2067 N  N   . PRO   A 1 280 ? -11.889 30.774  -25.574 1.00 31.22  ? 417 PRO   A N   1 
ATOM   2068 C  CA  . PRO   A 1 280 ? -10.613 30.674  -26.286 1.00 28.84  ? 417 PRO   A CA  1 
ATOM   2069 C  C   . PRO   A 1 280 ? -9.805  29.492  -25.775 1.00 30.76  ? 417 PRO   A C   1 
ATOM   2070 O  O   . PRO   A 1 280 ? -9.685  29.265  -24.567 1.00 29.28  ? 417 PRO   A O   1 
ATOM   2071 C  CB  . PRO   A 1 280 ? -9.918  32.004  -25.972 1.00 25.68  ? 417 PRO   A CB  1 
ATOM   2072 C  CG  . PRO   A 1 280 ? -10.512 32.432  -24.674 1.00 33.00  ? 417 PRO   A CG  1 
ATOM   2073 C  CD  . PRO   A 1 280 ? -11.924 31.914  -24.643 1.00 34.64  ? 417 PRO   A CD  1 
ATOM   2074 N  N   . CYS   A 1 281 ? -9.259  28.722  -26.710 1.00 28.49  ? 418 CYS   A N   1 
ATOM   2075 C  CA  . CYS   A 1 281 ? -8.476  27.550  -26.359 1.00 34.04  ? 418 CYS   A CA  1 
ATOM   2076 C  C   . CYS   A 1 281 ? -7.118  27.581  -27.040 1.00 34.25  ? 418 CYS   A C   1 
ATOM   2077 O  O   . CYS   A 1 281 ? -6.913  28.247  -28.056 1.00 29.39  ? 418 CYS   A O   1 
ATOM   2078 C  CB  . CYS   A 1 281 ? -9.199  26.249  -26.720 1.00 31.55  ? 418 CYS   A CB  1 
ATOM   2079 S  SG  . CYS   A 1 281 ? -10.875 26.137  -26.089 1.00 35.43  ? 418 CYS   A SG  1 
ATOM   2080 N  N   . LYS   A 1 282 ? -6.186  26.844  -26.454 1.00 32.08  ? 419 LYS   A N   1 
ATOM   2081 C  CA  . LYS   A 1 282 ? -4.890  26.623  -27.068 1.00 29.16  ? 419 LYS   A CA  1 
ATOM   2082 C  C   . LYS   A 1 282 ? -4.612  25.131  -27.063 1.00 31.71  ? 419 LYS   A C   1 
ATOM   2083 O  O   . LYS   A 1 282 ? -4.862  24.447  -26.064 1.00 29.44  ? 419 LYS   A O   1 
ATOM   2084 C  CB  . LYS   A 1 282 ? -3.774  27.364  -26.329 1.00 34.70  ? 419 LYS   A CB  1 
ATOM   2085 C  CG  . LYS   A 1 282 ? -3.801  28.873  -26.481 1.00 34.62  ? 419 LYS   A CG  1 
ATOM   2086 C  CD  . LYS   A 1 282 ? -3.923  29.509  -25.108 1.00 46.86  ? 419 LYS   A CD  1 
ATOM   2087 C  CE  . LYS   A 1 282 ? -3.319  30.903  -25.060 1.00 50.95  ? 419 LYS   A CE  1 
ATOM   2088 N  NZ  . LYS   A 1 282 ? -3.308  31.411  -23.655 1.00 51.89  ? 419 LYS   A NZ  1 
ATOM   2089 N  N   . ILE   A 1 283 ? -4.111  24.627  -28.185 1.00 30.99  ? 420 ILE   A N   1 
ATOM   2090 C  CA  . ILE   A 1 283 ? -3.581  23.272  -28.228 1.00 28.12  ? 420 ILE   A CA  1 
ATOM   2091 C  C   . ILE   A 1 283 ? -2.157  23.332  -27.700 1.00 32.41  ? 420 ILE   A C   1 
ATOM   2092 O  O   . ILE   A 1 283 ? -1.302  24.017  -28.271 1.00 31.32  ? 420 ILE   A O   1 
ATOM   2093 C  CB  . ILE   A 1 283 ? -3.624  22.696  -29.647 1.00 29.71  ? 420 ILE   A CB  1 
ATOM   2094 C  CG1 . ILE   A 1 283 ? -5.053  22.315  -30.016 1.00 26.34  ? 420 ILE   A CG1 1 
ATOM   2095 C  CG2 . ILE   A 1 283 ? -2.754  21.464  -29.731 1.00 34.22  ? 420 ILE   A CG2 1 
ATOM   2096 C  CD1 . ILE   A 1 283 ? -5.184  21.727  -31.388 1.00 32.29  ? 420 ILE   A CD1 1 
ATOM   2097 N  N   . LYS   A 1 284 ? -1.903  22.639  -26.598 1.00 26.14  ? 421 LYS   A N   1 
ATOM   2098 C  CA  . LYS   A 1 284 ? -0.607  22.730  -25.950 1.00 29.51  ? 421 LYS   A CA  1 
ATOM   2099 C  C   . LYS   A 1 284 ? 0.245   21.522  -26.306 1.00 31.97  ? 421 LYS   A C   1 
ATOM   2100 O  O   . LYS   A 1 284 ? -0.249  20.397  -26.438 1.00 28.47  ? 421 LYS   A O   1 
ATOM   2101 C  CB  . LYS   A 1 284 ? -0.743  22.839  -24.432 1.00 32.06  ? 421 LYS   A CB  1 
ATOM   2102 C  CG  . LYS   A 1 284 ? -0.410  24.227  -23.898 1.00 34.74  ? 421 LYS   A CG  1 
ATOM   2103 C  CD  . LYS   A 1 284 ? -0.605  24.322  -22.390 1.00 34.40  ? 421 LYS   A CD  1 
ATOM   2104 C  CE  . LYS   A 1 284 ? 0.724   24.364  -21.656 1.00 35.30  ? 421 LYS   A CE  1 
ATOM   2105 N  NZ  . LYS   A 1 284 ? 1.802   24.972  -22.486 1.00 39.47  ? 421 LYS   A NZ  1 
ATOM   2106 N  N   . GLN   A 1 285 ? 1.535   21.781  -26.482 1.00 29.97  ? 422 GLN   A N   1 
ATOM   2107 C  CA  . GLN   A 1 285 ? 2.514   20.748  -26.782 1.00 32.66  ? 422 GLN   A CA  1 
ATOM   2108 C  C   . GLN   A 1 285 ? 3.221   20.234  -25.543 1.00 33.03  ? 422 GLN   A C   1 
ATOM   2109 O  O   . GLN   A 1 285 ? 3.605   19.059  -25.496 1.00 37.71  ? 422 GLN   A O   1 
ATOM   2110 C  CB  . GLN   A 1 285 ? 3.563   21.290  -27.754 1.00 29.36  ? 422 GLN   A CB  1 
ATOM   2111 C  CG  . GLN   A 1 285 ? 3.303   20.964  -29.198 1.00 35.06  ? 422 GLN   A CG  1 
ATOM   2112 C  CD  . GLN   A 1 285 ? 4.352   21.558  -30.100 1.00 39.71  ? 422 GLN   A CD  1 
ATOM   2113 O  OE1 . GLN   A 1 285 ? 4.134   22.589  -30.734 1.00 40.18  ? 422 GLN   A OE1 1 
ATOM   2114 N  NE2 . GLN   A 1 285 ? 5.510   20.906  -30.164 1.00 36.29  ? 422 GLN   A NE2 1 
ATOM   2115 N  N   . ILE   A 1 286 ? 3.398   21.090  -24.544 1.00 29.33  ? 423 ILE   A N   1 
ATOM   2116 C  CA  . ILE   A 1 286 ? 4.118   20.757  -23.325 1.00 28.91  ? 423 ILE   A CA  1 
ATOM   2117 C  C   . ILE   A 1 286 ? 3.088   20.577  -22.222 1.00 34.41  ? 423 ILE   A C   1 
ATOM   2118 O  O   . ILE   A 1 286 ? 2.390   21.529  -21.847 1.00 32.14  ? 423 ILE   A O   1 
ATOM   2119 C  CB  . ILE   A 1 286 ? 5.149   21.836  -22.968 1.00 32.94  ? 423 ILE   A CB  1 
ATOM   2120 C  CG1 . ILE   A 1 286 ? 6.233   21.874  -24.044 1.00 34.48  ? 423 ILE   A CG1 1 
ATOM   2121 C  CG2 . ILE   A 1 286 ? 5.772   21.553  -21.606 1.00 32.06  ? 423 ILE   A CG2 1 
ATOM   2122 C  CD1 . ILE   A 1 286 ? 7.153   23.064  -23.952 1.00 35.74  ? 423 ILE   A CD1 1 
ATOM   2123 N  N   . ILE   A 1 287 ? 2.995   19.358  -21.703 1.00 34.29  ? 424 ILE   A N   1 
ATOM   2124 C  CA  . ILE   A 1 287 ? 1.897   18.950  -20.841 1.00 32.94  ? 424 ILE   A CA  1 
ATOM   2125 C  C   . ILE   A 1 287 ? 2.453   18.646  -19.460 1.00 35.75  ? 424 ILE   A C   1 
ATOM   2126 O  O   . ILE   A 1 287 ? 3.502   18.007  -19.337 1.00 40.11  ? 424 ILE   A O   1 
ATOM   2127 C  CB  . ILE   A 1 287 ? 1.177   17.712  -21.417 1.00 34.26  ? 424 ILE   A CB  1 
ATOM   2128 C  CG1 . ILE   A 1 287 ? 0.721   17.995  -22.848 1.00 34.31  ? 424 ILE   A CG1 1 
ATOM   2129 C  CG2 . ILE   A 1 287 ? 0.004   17.301  -20.534 1.00 34.09  ? 424 ILE   A CG2 1 
ATOM   2130 C  CD1 . ILE   A 1 287 ? -0.181  19.179  -22.960 1.00 30.19  ? 424 ILE   A CD1 1 
ATOM   2131 N  N   . ASN   A 1 288 ? 1.759   19.103  -18.424 1.00 32.14  ? 425 ASN   A N   1 
ATOM   2132 C  CA  . ASN   A 1 288 ? 1.979   18.589  -17.077 1.00 34.96  ? 425 ASN   A CA  1 
ATOM   2133 C  C   . ASN   A 1 288 ? 1.082   17.369  -16.911 1.00 37.23  ? 425 ASN   A C   1 
ATOM   2134 O  O   . ASN   A 1 288 ? -0.143  17.497  -16.782 1.00 35.86  ? 425 ASN   A O   1 
ATOM   2135 C  CB  . ASN   A 1 288 ? 1.707   19.656  -16.023 1.00 38.47  ? 425 ASN   A CB  1 
ATOM   2136 C  CG  . ASN   A 1 288 ? 2.617   20.858  -16.169 1.00 37.63  ? 425 ASN   A CG  1 
ATOM   2137 O  OD1 . ASN   A 1 288 ? 3.837   20.714  -16.240 1.00 39.10  ? 425 ASN   A OD1 1 
ATOM   2138 N  ND2 . ASN   A 1 288 ? 2.034   22.048  -16.209 1.00 34.81  ? 425 ASN   A ND2 1 
ATOM   2139 N  N   . MET   A 1 289 ? 1.698   16.189  -16.935 1.00 34.32  ? 426 MET   A N   1 
ATOM   2140 C  CA  . MET   A 1 289 ? 0.954   14.954  -17.117 1.00 33.21  ? 426 MET   A CA  1 
ATOM   2141 C  C   . MET   A 1 289 ? 0.082   14.656  -15.903 1.00 30.82  ? 426 MET   A C   1 
ATOM   2142 O  O   . MET   A 1 289 ? 0.456   14.916  -14.756 1.00 33.71  ? 426 MET   A O   1 
ATOM   2143 C  CB  . MET   A 1 289 ? 1.915   13.805  -17.353 1.00 36.51  ? 426 MET   A CB  1 
ATOM   2144 C  CG  . MET   A 1 289 ? 2.481   13.719  -18.760 1.00 38.90  ? 426 MET   A CG  1 
ATOM   2145 S  SD  . MET   A 1 289 ? 3.604   12.312  -18.907 1.00 56.20  ? 426 MET   A SD  1 
ATOM   2146 C  CE  . MET   A 1 289 ? 4.924   12.832  -17.806 1.00 42.81  ? 426 MET   A CE  1 
ATOM   2147 N  N   . TRP   A 1 290 ? -1.089  14.078  -16.160 1.00 27.25  ? 427 TRP   A N   1 
ATOM   2148 C  CA  . TRP   A 1 290 ? -1.945  13.690  -15.050 1.00 30.96  ? 427 TRP   A CA  1 
ATOM   2149 C  C   . TRP   A 1 290 ? -1.496  12.380  -14.422 1.00 33.57  ? 427 TRP   A C   1 
ATOM   2150 O  O   . TRP   A 1 290 ? -1.834  12.113  -13.263 1.00 32.76  ? 427 TRP   A O   1 
ATOM   2151 C  CB  . TRP   A 1 290 ? -3.386  13.536  -15.518 1.00 30.05  ? 427 TRP   A CB  1 
ATOM   2152 C  CG  . TRP   A 1 290 ? -3.554  12.531  -16.611 1.00 26.50  ? 427 TRP   A CG  1 
ATOM   2153 C  CD1 . TRP   A 1 290 ? -3.427  12.732  -17.957 1.00 26.82  ? 427 TRP   A CD1 1 
ATOM   2154 C  CD2 . TRP   A 1 290 ? -3.873  11.152  -16.439 1.00 31.50  ? 427 TRP   A CD2 1 
ATOM   2155 N  NE1 . TRP   A 1 290 ? -3.656  11.559  -18.630 1.00 30.17  ? 427 TRP   A NE1 1 
ATOM   2156 C  CE2 . TRP   A 1 290 ? -3.932  10.574  -17.718 1.00 30.33  ? 427 TRP   A CE2 1 
ATOM   2157 C  CE3 . TRP   A 1 290 ? -4.116  10.346  -15.321 1.00 31.74  ? 427 TRP   A CE3 1 
ATOM   2158 C  CZ2 . TRP   A 1 290 ? -4.241  9.239   -17.911 1.00 28.47  ? 427 TRP   A CZ2 1 
ATOM   2159 C  CZ3 . TRP   A 1 290 ? -4.411  9.017   -15.514 1.00 29.07  ? 427 TRP   A CZ3 1 
ATOM   2160 C  CH2 . TRP   A 1 290 ? -4.465  8.473   -16.797 1.00 28.10  ? 427 TRP   A CH2 1 
ATOM   2161 N  N   . GLN   A 1 291 ? -0.748  11.562  -15.170 1.00 31.04  ? 428 GLN   A N   1 
ATOM   2162 C  CA  . GLN   A 1 291 ? -0.371  10.236  -14.690 1.00 32.53  ? 428 GLN   A CA  1 
ATOM   2163 C  C   . GLN   A 1 291 ? 0.469   10.326  -13.423 1.00 37.17  ? 428 GLN   A C   1 
ATOM   2164 O  O   . GLN   A 1 291 ? 0.361   9.480   -12.528 1.00 45.20  ? 428 GLN   A O   1 
ATOM   2165 C  CB  . GLN   A 1 291 ? 0.404   9.494   -15.775 1.00 31.38  ? 428 GLN   A CB  1 
ATOM   2166 C  CG  . GLN   A 1 291 ? -0.395  9.150   -17.018 1.00 31.46  ? 428 GLN   A CG  1 
ATOM   2167 C  CD  . GLN   A 1 291 ? -0.261  10.206  -18.099 1.00 33.84  ? 428 GLN   A CD  1 
ATOM   2168 O  OE1 . GLN   A 1 291 ? -0.293  11.410  -17.821 1.00 33.51  ? 428 GLN   A OE1 1 
ATOM   2169 N  NE2 . GLN   A 1 291 ? -0.088  9.760   -19.340 1.00 33.23  ? 428 GLN   A NE2 1 
ATOM   2170 N  N   . GLY   A 1 292 ? 1.302   11.349  -13.335 1.00 37.95  ? 429 GLY   A N   1 
ATOM   2171 C  CA  . GLY   A 1 292 ? 2.289   11.461  -12.285 1.00 45.07  ? 429 GLY   A CA  1 
ATOM   2172 C  C   . GLY   A 1 292 ? 3.260   12.545  -12.674 1.00 44.91  ? 429 GLY   A C   1 
ATOM   2173 O  O   . GLY   A 1 292 ? 3.301   12.988  -13.826 1.00 47.22  ? 429 GLY   A O   1 
ATOM   2174 N  N   . THR   A 1 293 ? 4.036   12.979  -11.684 1.00 47.66  ? 430 THR   A N   1 
ATOM   2175 C  CA  . THR   A 1 293 ? 4.899   14.143  -11.857 1.00 56.45  ? 430 THR   A CA  1 
ATOM   2176 C  C   . THR   A 1 293 ? 5.748   14.004  -13.115 1.00 52.99  ? 430 THR   A C   1 
ATOM   2177 O  O   . THR   A 1 293 ? 6.357   12.957  -13.358 1.00 54.61  ? 430 THR   A O   1 
ATOM   2178 C  CB  . THR   A 1 293 ? 5.775   14.331  -10.611 1.00 65.84  ? 430 THR   A CB  1 
ATOM   2179 O  OG1 . THR   A 1 293 ? 5.327   15.491  -9.904  1.00 62.65  ? 430 THR   A OG1 1 
ATOM   2180 C  CG2 . THR   A 1 293 ? 7.245   14.538  -10.976 1.00 69.11  ? 430 THR   A CG2 1 
ATOM   2181 N  N   . GLY   A 1 294 ? 5.730   15.031  -13.941 1.00 49.20  ? 431 GLY   A N   1 
ATOM   2182 C  CA  . GLY   A 1 294 ? 6.459   15.026  -15.195 1.00 51.45  ? 431 GLY   A CA  1 
ATOM   2183 C  C   . GLY   A 1 294 ? 5.798   15.913  -16.239 1.00 44.01  ? 431 GLY   A C   1 
ATOM   2184 O  O   . GLY   A 1 294 ? 4.580   16.046  -16.321 1.00 41.48  ? 431 GLY   A O   1 
ATOM   2185 N  N   . GLN   A 1 295 ? 6.635   16.564  -17.042 1.00 42.08  ? 432 GLN   A N   1 
ATOM   2186 C  CA  . GLN   A 1 295 ? 6.208   17.305  -18.221 1.00 44.81  ? 432 GLN   A CA  1 
ATOM   2187 C  C   . GLN   A 1 295 ? 6.439   16.442  -19.452 1.00 43.88  ? 432 GLN   A C   1 
ATOM   2188 O  O   . GLN   A 1 295 ? 7.533   15.901  -19.629 1.00 52.10  ? 432 GLN   A O   1 
ATOM   2189 C  CB  . GLN   A 1 295 ? 6.996   18.603  -18.392 1.00 46.66  ? 432 GLN   A CB  1 
ATOM   2190 C  CG  . GLN   A 1 295 ? 6.450   19.832  -17.733 1.00 47.79  ? 432 GLN   A CG  1 
ATOM   2191 C  CD  . GLN   A 1 295 ? 7.521   20.888  -17.621 1.00 52.87  ? 432 GLN   A CD  1 
ATOM   2192 O  OE1 . GLN   A 1 295 ? 8.328   21.056  -18.538 1.00 52.84  ? 432 GLN   A OE1 1 
ATOM   2193 N  NE2 . GLN   A 1 295 ? 7.561   21.585  -16.490 1.00 56.90  ? 432 GLN   A NE2 1 
ATOM   2194 N  N   . ALA   A 1 296 ? 5.431   16.332  -20.309 1.00 39.72  ? 433 ALA   A N   1 
ATOM   2195 C  CA  . ALA   A 1 296 ? 5.562   15.638  -21.583 1.00 40.56  ? 433 ALA   A CA  1 
ATOM   2196 C  C   . ALA   A 1 296 ? 5.425   16.643  -22.716 1.00 40.09  ? 433 ALA   A C   1 
ATOM   2197 O  O   . ALA   A 1 296 ? 4.569   17.532  -22.662 1.00 41.65  ? 433 ALA   A O   1 
ATOM   2198 C  CB  . ALA   A 1 296 ? 4.510   14.536  -21.728 1.00 38.73  ? 433 ALA   A CB  1 
ATOM   2199 N  N   . MET   A 1 297 ? 6.263   16.508  -23.745 1.00 36.26  ? 434 MET   A N   1 
ATOM   2200 C  CA  . MET   A 1 297 ? 6.212   17.385  -24.909 1.00 35.67  ? 434 MET   A CA  1 
ATOM   2201 C  C   . MET   A 1 297 ? 5.818   16.582  -26.137 1.00 33.56  ? 434 MET   A C   1 
ATOM   2202 O  O   . MET   A 1 297 ? 6.482   15.599  -26.479 1.00 38.00  ? 434 MET   A O   1 
ATOM   2203 C  CB  . MET   A 1 297 ? 7.544   18.090  -25.160 1.00 37.00  ? 434 MET   A CB  1 
ATOM   2204 C  CG  . MET   A 1 297 ? 7.363   19.285  -26.088 1.00 36.25  ? 434 MET   A CG  1 
ATOM   2205 S  SD  . MET   A 1 297 ? 8.866   20.072  -26.688 1.00 48.62  ? 434 MET   A SD  1 
ATOM   2206 C  CE  . MET   A 1 297 ? 9.243   19.034  -28.100 1.00 47.38  ? 434 MET   A CE  1 
ATOM   2207 N  N   . TYR   A 1 298 ? 4.753   17.012  -26.802 1.00 33.22  ? 435 TYR   A N   1 
ATOM   2208 C  CA  . TYR   A 1 298 ? 4.236   16.348  -27.984 1.00 30.10  ? 435 TYR   A CA  1 
ATOM   2209 C  C   . TYR   A 1 298 ? 4.539   17.193  -29.214 1.00 35.51  ? 435 TYR   A C   1 
ATOM   2210 O  O   . TYR   A 1 298 ? 5.026   18.324  -29.122 1.00 35.43  ? 435 TYR   A O   1 
ATOM   2211 C  CB  . TYR   A 1 298 ? 2.732   16.087  -27.844 1.00 33.04  ? 435 TYR   A CB  1 
ATOM   2212 C  CG  . TYR   A 1 298 ? 2.410   15.074  -26.772 1.00 33.98  ? 435 TYR   A CG  1 
ATOM   2213 C  CD1 . TYR   A 1 298 ? 2.445   15.422  -25.427 1.00 31.52  ? 435 TYR   A CD1 1 
ATOM   2214 C  CD2 . TYR   A 1 298 ? 2.108   13.761  -27.102 1.00 37.58  ? 435 TYR   A CD2 1 
ATOM   2215 C  CE1 . TYR   A 1 298 ? 2.166   14.494  -24.444 1.00 33.57  ? 435 TYR   A CE1 1 
ATOM   2216 C  CE2 . TYR   A 1 298 ? 1.830   12.823  -26.127 1.00 36.55  ? 435 TYR   A CE2 1 
ATOM   2217 C  CZ  . TYR   A 1 298 ? 1.861   13.197  -24.799 1.00 37.36  ? 435 TYR   A CZ  1 
ATOM   2218 O  OH  . TYR   A 1 298 ? 1.585   12.279  -23.811 1.00 37.42  ? 435 TYR   A OH  1 
ATOM   2219 N  N   . ALA   A 1 299 ? 4.247   16.621  -30.372 1.00 38.35  ? 436 ALA   A N   1 
ATOM   2220 C  CA  . ALA   A 1 299 ? 4.447   17.283  -31.644 1.00 34.59  ? 436 ALA   A CA  1 
ATOM   2221 C  C   . ALA   A 1 299 ? 3.381   18.356  -31.858 1.00 37.54  ? 436 ALA   A C   1 
ATOM   2222 O  O   . ALA   A 1 299 ? 2.334   18.345  -31.202 1.00 34.98  ? 436 ALA   A O   1 
ATOM   2223 C  CB  . ALA   A 1 299 ? 4.408   16.253  -32.768 1.00 42.53  ? 436 ALA   A CB  1 
ATOM   2224 N  N   . PRO   A 1 300 ? 3.619   19.300  -32.770 1.00 38.86  ? 437 PRO   A N   1 
ATOM   2225 C  CA  . PRO   A 1 300 ? 2.583   20.298  -33.103 1.00 38.12  ? 437 PRO   A CA  1 
ATOM   2226 C  C   . PRO   A 1 300 ? 1.351   19.637  -33.694 1.00 38.00  ? 437 PRO   A C   1 
ATOM   2227 O  O   . PRO   A 1 300 ? 1.416   18.487  -34.155 1.00 39.74  ? 437 PRO   A O   1 
ATOM   2228 C  CB  . PRO   A 1 300 ? 3.288   21.221  -34.115 1.00 39.85  ? 437 PRO   A CB  1 
ATOM   2229 C  CG  . PRO   A 1 300 ? 4.743   20.952  -33.923 1.00 38.70  ? 437 PRO   A CG  1 
ATOM   2230 C  CD  . PRO   A 1 300 ? 4.838   19.514  -33.566 1.00 38.68  ? 437 PRO   A CD  1 
ATOM   2231 N  N   . PRO   A 1 301 ? 0.206   20.319  -33.666 1.00 38.03  ? 438 PRO   A N   1 
ATOM   2232 C  CA  . PRO   A 1 301 ? -1.051  19.655  -34.019 1.00 40.26  ? 438 PRO   A CA  1 
ATOM   2233 C  C   . PRO   A 1 301 ? -1.052  19.109  -35.440 1.00 41.65  ? 438 PRO   A C   1 
ATOM   2234 O  O   . PRO   A 1 301 ? -0.265  19.510  -36.304 1.00 44.86  ? 438 PRO   A O   1 
ATOM   2235 C  CB  . PRO   A 1 301 ? -2.105  20.758  -33.842 1.00 40.01  ? 438 PRO   A CB  1 
ATOM   2236 C  CG  . PRO   A 1 301 ? -1.344  22.041  -33.630 1.00 35.34  ? 438 PRO   A CG  1 
ATOM   2237 C  CD  . PRO   A 1 301 ? -0.005  21.671  -33.115 1.00 37.83  ? 438 PRO   A CD  1 
ATOM   2238 N  N   . ILE   A 1 302 ? -1.953  18.151  -35.660 1.00 41.05  ? 439 ILE   A N   1 
ATOM   2239 C  CA  . ILE   A 1 302 ? -2.197  17.598  -36.983 1.00 40.11  ? 439 ILE   A CA  1 
ATOM   2240 C  C   . ILE   A 1 302 ? -2.814  18.689  -37.842 1.00 41.85  ? 439 ILE   A C   1 
ATOM   2241 O  O   . ILE   A 1 302 ? -3.274  19.714  -37.326 1.00 40.26  ? 439 ILE   A O   1 
ATOM   2242 C  CB  . ILE   A 1 302 ? -3.132  16.378  -36.936 1.00 36.96  ? 439 ILE   A CB  1 
ATOM   2243 C  CG1 . ILE   A 1 302 ? -4.484  16.784  -36.343 1.00 39.96  ? 439 ILE   A CG1 1 
ATOM   2244 C  CG2 . ILE   A 1 302 ? -2.502  15.230  -36.169 1.00 41.03  ? 439 ILE   A CG2 1 
ATOM   2245 C  CD1 . ILE   A 1 302 ? -5.427  15.622  -36.082 1.00 36.53  ? 439 ILE   A CD1 1 
ATOM   2246 N  N   . ASP   A 1 303 ? -2.844  18.470  -39.152 1.00 45.64  ? 440 ASP   A N   1 
ATOM   2247 C  CA  . ASP   A 1 303 ? -3.517  19.395  -40.047 1.00 41.81  ? 440 ASP   A CA  1 
ATOM   2248 C  C   . ASP   A 1 303 ? -5.018  19.104  -40.072 1.00 43.08  ? 440 ASP   A C   1 
ATOM   2249 O  O   . ASP   A 1 303 ? -5.483  18.048  -39.630 1.00 41.49  ? 440 ASP   A O   1 
ATOM   2250 C  CB  . ASP   A 1 303 ? -2.921  19.297  -41.452 1.00 42.34  ? 440 ASP   A CB  1 
ATOM   2251 C  CG  . ASP   A 1 303 ? -1.476  19.759  -41.499 1.00 50.45  ? 440 ASP   A CG  1 
ATOM   2252 O  OD1 . ASP   A 1 303 ? -1.143  20.759  -40.826 1.00 51.92  ? 440 ASP   A OD1 1 
ATOM   2253 O  OD2 . ASP   A 1 303 ? -0.662  19.114  -42.196 1.00 52.64  ? 440 ASP   A OD2 1 
ATOM   2254 N  N   . GLY   A 1 304 ? -5.779  20.074  -40.570 1.00 38.26  ? 441 GLY   A N   1 
ATOM   2255 C  CA  . GLY   A 1 304 ? -7.209  19.921  -40.759 1.00 37.73  ? 441 GLY   A CA  1 
ATOM   2256 C  C   . GLY   A 1 304 ? -8.006  20.476  -39.590 1.00 39.11  ? 441 GLY   A C   1 
ATOM   2257 O  O   . GLY   A 1 304 ? -7.470  20.971  -38.592 1.00 40.03  ? 441 GLY   A O   1 
ATOM   2258 N  N   . LYS   A 1 305 ? -9.328  20.402  -39.754 1.00 39.07  ? 442 LYS   A N   1 
ATOM   2259 C  CA  . LYS   A 1 305 ? -10.293 20.808  -38.734 1.00 41.36  ? 442 LYS   A CA  1 
ATOM   2260 C  C   . LYS   A 1 305 ? -10.267 19.786  -37.601 1.00 35.70  ? 442 LYS   A C   1 
ATOM   2261 O  O   . LYS   A 1 305 ? -10.711 18.649  -37.782 1.00 41.82  ? 442 LYS   A O   1 
ATOM   2262 C  CB  . LYS   A 1 305 ? -11.690 20.878  -39.350 1.00 44.47  ? 442 LYS   A CB  1 
ATOM   2263 C  CG  . LYS   A 1 305 ? -12.787 21.452  -38.454 1.00 40.30  ? 442 LYS   A CG  1 
ATOM   2264 C  CD  . LYS   A 1 305 ? -13.130 22.926  -38.705 1.00 48.18  ? 442 LYS   A CD  1 
ATOM   2265 C  CE  . LYS   A 1 305 ? -12.592 23.469  -40.025 1.00 45.99  ? 442 LYS   A CE  1 
ATOM   2266 N  NZ  . LYS   A 1 305 ? -11.908 24.788  -39.924 1.00 41.71  ? 442 LYS   A NZ  1 
ATOM   2267 N  N   . ILE   A 1 306 ? -9.740  20.163  -36.438 1.00 36.08  ? 443 ILE   A N   1 
ATOM   2268 C  CA  . ILE   A 1 306 ? -9.724  19.281  -35.271 1.00 32.46  ? 443 ILE   A CA  1 
ATOM   2269 C  C   . ILE   A 1 306 ? -10.958 19.602  -34.438 1.00 34.71  ? 443 ILE   A C   1 
ATOM   2270 O  O   . ILE   A 1 306 ? -11.023 20.654  -33.799 1.00 33.00  ? 443 ILE   A O   1 
ATOM   2271 C  CB  . ILE   A 1 306 ? -8.446  19.453  -34.441 1.00 33.60  ? 443 ILE   A CB  1 
ATOM   2272 C  CG1 . ILE   A 1 306 ? -7.202  19.223  -35.292 1.00 30.17  ? 443 ILE   A CG1 1 
ATOM   2273 C  CG2 . ILE   A 1 306 ? -8.444  18.492  -33.269 1.00 33.83  ? 443 ILE   A CG2 1 
ATOM   2274 C  CD1 . ILE   A 1 306 ? -5.915  19.673  -34.621 1.00 37.21  ? 443 ILE   A CD1 1 
ATOM   2275 N  N   . ASN   A 1 307 ? -11.931 18.696  -34.419 1.00 33.08  ? 444 ASN   A N   1 
ATOM   2276 C  CA  . ASN   A 1 307 ? -13.213 18.985  -33.794 1.00 34.86  ? 444 ASN   A CA  1 
ATOM   2277 C  C   . ASN   A 1 307 ? -13.626 17.841  -32.883 1.00 35.63  ? 444 ASN   A C   1 
ATOM   2278 O  O   . ASN   A 1 307 ? -13.600 16.676  -33.293 1.00 36.41  ? 444 ASN   A O   1 
ATOM   2279 C  CB  . ASN   A 1 307 ? -14.293 19.240  -34.852 1.00 36.92  ? 444 ASN   A CB  1 
ATOM   2280 C  CG  . ASN   A 1 307 ? -15.676 19.383  -34.249 1.00 39.27  ? 444 ASN   A CG  1 
ATOM   2281 O  OD1 . ASN   A 1 307 ? -16.509 18.481  -34.353 1.00 39.23  ? 444 ASN   A OD1 1 
ATOM   2282 N  ND2 . ASN   A 1 307 ? -15.926 20.521  -33.608 1.00 37.99  ? 444 ASN   A ND2 1 
ATOM   2283 N  N   . CYS   A 1 308 ? -14.004 18.181  -31.649 1.00 38.05  ? 445 CYS   A N   1 
ATOM   2284 C  CA  . CYS   A 1 308 ? -14.589 17.240  -30.701 1.00 35.70  ? 445 CYS   A CA  1 
ATOM   2285 C  C   . CYS   A 1 308 ? -15.846 17.868  -30.129 1.00 33.55  ? 445 CYS   A C   1 
ATOM   2286 O  O   . CYS   A 1 308 ? -15.787 18.951  -29.538 1.00 31.41  ? 445 CYS   A O   1 
ATOM   2287 C  CB  . CYS   A 1 308 ? -13.623 16.897  -29.566 1.00 37.27  ? 445 CYS   A CB  1 
ATOM   2288 S  SG  . CYS   A 1 308 ? -12.249 15.855  -30.038 1.00 35.95  ? 445 CYS   A SG  1 
ATOM   2289 N  N   . VAL   A 1 309 ? -16.975 17.199  -30.311 1.00 35.53  ? 446 VAL   A N   1 
ATOM   2290 C  CA  . VAL   A 1 309 ? -18.235 17.597  -29.700 1.00 33.52  ? 446 VAL   A CA  1 
ATOM   2291 C  C   . VAL   A 1 309 ? -18.458 16.681  -28.506 1.00 32.76  ? 446 VAL   A C   1 
ATOM   2292 O  O   . VAL   A 1 309 ? -18.671 15.476  -28.669 1.00 28.76  ? 446 VAL   A O   1 
ATOM   2293 C  CB  . VAL   A 1 309 ? -19.398 17.516  -30.695 1.00 32.23  ? 446 VAL   A CB  1 
ATOM   2294 C  CG1 . VAL   A 1 309 ? -20.667 18.030  -30.052 1.00 36.97  ? 446 VAL   A CG1 1 
ATOM   2295 C  CG2 . VAL   A 1 309 ? -19.077 18.316  -31.946 1.00 35.23  ? 446 VAL   A CG2 1 
ATOM   2296 N  N   . SER   A 1 310 ? -18.398 17.243  -27.304 1.00 32.80  ? 447 SER   A N   1 
ATOM   2297 C  CA  . SER   A 1 310 ? -18.509 16.465  -26.082 1.00 30.22  ? 447 SER   A CA  1 
ATOM   2298 C  C   . SER   A 1 310 ? -19.705 16.927  -25.263 1.00 30.07  ? 447 SER   A C   1 
ATOM   2299 O  O   . SER   A 1 310 ? -20.135 18.082  -25.345 1.00 34.91  ? 447 SER   A O   1 
ATOM   2300 C  CB  . SER   A 1 310 ? -17.234 16.562  -25.229 1.00 31.95  ? 447 SER   A CB  1 
ATOM   2301 O  OG  . SER   A 1 310 ? -16.073 16.574  -26.044 1.00 33.37  ? 447 SER   A OG  1 
ATOM   2302 N  N   . ASN   A 1 311 ? -20.235 16.004  -24.471 1.00 25.46  ? 448 ASN   A N   1 
ATOM   2303 C  CA  . ASN   A 1 311 ? -21.242 16.318  -23.472 1.00 29.40  ? 448 ASN   A CA  1 
ATOM   2304 C  C   . ASN   A 1 311 ? -20.554 16.681  -22.166 1.00 30.83  ? 448 ASN   A C   1 
ATOM   2305 O  O   . ASN   A 1 311 ? -19.761 15.894  -21.643 1.00 32.20  ? 448 ASN   A O   1 
ATOM   2306 C  CB  . ASN   A 1 311 ? -22.155 15.121  -23.233 1.00 36.42  ? 448 ASN   A CB  1 
ATOM   2307 C  CG  . ASN   A 1 311 ? -23.206 14.954  -24.294 1.00 42.91  ? 448 ASN   A CG  1 
ATOM   2308 O  OD1 . ASN   A 1 311 ? -23.578 15.895  -24.993 1.00 43.17  ? 448 ASN   A OD1 1 
ATOM   2309 N  ND2 . ASN   A 1 311 ? -23.688 13.730  -24.420 1.00 50.91  ? 448 ASN   A ND2 1 
ATOM   2310 N  N   . ILE   A 1 312 ? -20.850 17.864  -21.643 1.00 29.50  ? 449 ILE   A N   1 
ATOM   2311 C  CA  . ILE   A 1 312 ? -20.510 18.169  -20.261 1.00 32.23  ? 449 ILE   A CA  1 
ATOM   2312 C  C   . ILE   A 1 312 ? -21.519 17.432  -19.394 1.00 31.69  ? 449 ILE   A C   1 
ATOM   2313 O  O   . ILE   A 1 312 ? -22.720 17.710  -19.457 1.00 31.83  ? 449 ILE   A O   1 
ATOM   2314 C  CB  . ILE   A 1 312 ? -20.544 19.679  -19.991 1.00 29.86  ? 449 ILE   A CB  1 
ATOM   2315 C  CG1 . ILE   A 1 312 ? -19.521 20.410  -20.860 1.00 32.59  ? 449 ILE   A CG1 1 
ATOM   2316 C  CG2 . ILE   A 1 312 ? -20.241 19.954  -18.544 1.00 29.65  ? 449 ILE   A CG2 1 
ATOM   2317 C  CD1 . ILE   A 1 312 ? -19.706 21.910  -20.873 1.00 32.22  ? 449 ILE   A CD1 1 
ATOM   2318 N  N   . THR   A 1 313 ? -21.044 16.464  -18.619 1.00 29.83  ? 450 THR   A N   1 
ATOM   2319 C  CA  . THR   A 1 313 ? -21.918 15.682  -17.762 1.00 31.37  ? 450 THR   A CA  1 
ATOM   2320 C  C   . THR   A 1 313 ? -21.599 15.845  -16.289 1.00 31.64  ? 450 THR   A C   1 
ATOM   2321 O  O   . THR   A 1 313 ? -22.353 15.340  -15.448 1.00 35.89  ? 450 THR   A O   1 
ATOM   2322 C  CB  . THR   A 1 313 ? -21.837 14.195  -18.129 1.00 31.67  ? 450 THR   A CB  1 
ATOM   2323 O  OG1 . THR   A 1 313 ? -20.471 13.774  -18.077 1.00 32.36  ? 450 THR   A OG1 1 
ATOM   2324 C  CG2 . THR   A 1 313 ? -22.364 13.978  -19.535 1.00 32.88  ? 450 THR   A CG2 1 
ATOM   2325 N  N   . GLY   A 1 314 ? -20.513 16.526  -15.957 1.00 30.12  ? 451 GLY   A N   1 
ATOM   2326 C  CA  . GLY   A 1 314 ? -20.145 16.738  -14.575 1.00 26.61  ? 451 GLY   A CA  1 
ATOM   2327 C  C   . GLY   A 1 314 ? -19.236 17.936  -14.460 1.00 32.23  ? 451 GLY   A C   1 
ATOM   2328 O  O   . GLY   A 1 314 ? -18.673 18.411  -15.451 1.00 29.85  ? 451 GLY   A O   1 
ATOM   2329 N  N   . ILE   A 1 315 ? -19.109 18.436  -13.235 1.00 31.25  ? 452 ILE   A N   1 
ATOM   2330 C  CA  . ILE   A 1 315 ? -18.211 19.544  -12.936 1.00 29.00  ? 452 ILE   A CA  1 
ATOM   2331 C  C   . ILE   A 1 315 ? -17.390 19.189  -11.707 1.00 30.44  ? 452 ILE   A C   1 
ATOM   2332 O  O   . ILE   A 1 315 ? -17.924 18.666  -10.724 1.00 31.11  ? 452 ILE   A O   1 
ATOM   2333 C  CB  . ILE   A 1 315 ? -18.958 20.875  -12.706 1.00 26.42  ? 452 ILE   A CB  1 
ATOM   2334 C  CG1 . ILE   A 1 315 ? -19.994 21.121  -13.804 1.00 27.42  ? 452 ILE   A CG1 1 
ATOM   2335 C  CG2 . ILE   A 1 315 ? -17.965 22.030  -12.649 1.00 28.92  ? 452 ILE   A CG2 1 
ATOM   2336 C  CD1 . ILE   A 1 315 ? -20.938 22.258  -13.495 1.00 27.33  ? 452 ILE   A CD1 1 
ATOM   2337 N  N   . LEU   A 1 316 ? -16.093 19.468  -11.768 1.00 26.68  ? 453 LEU   A N   1 
ATOM   2338 C  CA  . LEU   A 1 316 ? -15.192 19.282  -10.639 1.00 29.53  ? 453 LEU   A CA  1 
ATOM   2339 C  C   . LEU   A 1 316 ? -15.045 20.627  -9.943  1.00 30.25  ? 453 LEU   A C   1 
ATOM   2340 O  O   . LEU   A 1 316 ? -14.672 21.616  -10.581 1.00 30.49  ? 453 LEU   A O   1 
ATOM   2341 C  CB  . LEU   A 1 316 ? -13.834 18.752  -11.104 1.00 31.12  ? 453 LEU   A CB  1 
ATOM   2342 C  CG  . LEU   A 1 316 ? -13.883 17.345  -11.708 1.00 28.79  ? 453 LEU   A CG  1 
ATOM   2343 C  CD1 . LEU   A 1 316 ? -12.556 16.987  -12.362 1.00 33.68  ? 453 LEU   A CD1 1 
ATOM   2344 C  CD2 . LEU   A 1 316 ? -14.273 16.302  -10.660 1.00 31.96  ? 453 LEU   A CD2 1 
ATOM   2345 N  N   . LEU   A 1 317 ? -15.357 20.675  -8.650  1.00 28.90  ? 454 LEU   A N   1 
ATOM   2346 C  CA  . LEU   A 1 317 ? -15.378 21.936  -7.923  1.00 32.30  ? 454 LEU   A CA  1 
ATOM   2347 C  C   . LEU   A 1 317 ? -14.579 21.830  -6.635  1.00 30.72  ? 454 LEU   A C   1 
ATOM   2348 O  O   . LEU   A 1 317 ? -14.562 20.789  -5.971  1.00 30.52  ? 454 LEU   A O   1 
ATOM   2349 C  CB  . LEU   A 1 317 ? -16.805 22.383  -7.587  1.00 28.62  ? 454 LEU   A CB  1 
ATOM   2350 C  CG  . LEU   A 1 317 ? -17.745 22.754  -8.732  1.00 31.80  ? 454 LEU   A CG  1 
ATOM   2351 C  CD1 . LEU   A 1 317 ? -19.125 23.076  -8.179  1.00 30.57  ? 454 LEU   A CD1 1 
ATOM   2352 C  CD2 . LEU   A 1 317 ? -17.189 23.921  -9.538  1.00 29.83  ? 454 LEU   A CD2 1 
ATOM   2353 N  N   . THR   A 1 318 ? -13.929 22.936  -6.288  1.00 32.20  ? 455 THR   A N   1 
ATOM   2354 C  CA  . THR   A 1 318 ? -13.261 23.111  -5.009  1.00 31.22  ? 455 THR   A CA  1 
ATOM   2355 C  C   . THR   A 1 318 ? -13.861 24.335  -4.337  1.00 35.49  ? 455 THR   A C   1 
ATOM   2356 O  O   . THR   A 1 318 ? -13.997 25.388  -4.969  1.00 37.41  ? 455 THR   A O   1 
ATOM   2357 C  CB  . THR   A 1 318 ? -11.758 23.291  -5.194  1.00 33.13  ? 455 THR   A CB  1 
ATOM   2358 O  OG1 . THR   A 1 318 ? -11.222 22.136  -5.850  1.00 39.32  ? 455 THR   A OG1 1 
ATOM   2359 C  CG2 . THR   A 1 318 ? -11.083 23.452  -3.848  1.00 34.60  ? 455 THR   A CG2 1 
ATOM   2360 N  N   . ARG   A 1 319 ? -14.242 24.189  -3.073  1.00 38.04  ? 456 ARG   A N   1 
ATOM   2361 C  CA  . ARG   A 1 319 ? -14.885 25.268  -2.341  1.00 35.26  ? 456 ARG   A CA  1 
ATOM   2362 C  C   . ARG   A 1 319 ? -13.848 26.031  -1.530  1.00 37.28  ? 456 ARG   A C   1 
ATOM   2363 O  O   . ARG   A 1 319 ? -13.009 25.430  -0.853  1.00 36.48  ? 456 ARG   A O   1 
ATOM   2364 C  CB  . ARG   A 1 319 ? -15.986 24.724  -1.427  1.00 40.34  ? 456 ARG   A CB  1 
ATOM   2365 C  CG  . ARG   A 1 319 ? -16.793 25.813  -0.721  1.00 37.53  ? 456 ARG   A CG  1 
ATOM   2366 C  CD  . ARG   A 1 319 ? -17.887 25.230  0.164   1.00 41.88  ? 456 ARG   A CD  1 
ATOM   2367 N  NE  . ARG   A 1 319 ? -17.408 24.189  1.066   1.00 34.99  ? 456 ARG   A NE  1 
ATOM   2368 C  CZ  . ARG   A 1 319 ? -17.029 24.409  2.318   1.00 39.06  ? 456 ARG   A CZ  1 
ATOM   2369 N  NH1 . ARG   A 1 319 ? -17.079 25.619  2.851   1.00 41.90  ? 456 ARG   A NH1 1 
ATOM   2370 N  NH2 . ARG   A 1 319 ? -16.592 23.392  3.053   1.00 41.22  ? 456 ARG   A NH2 1 
ATOM   2371 N  N   . ASP   A 1 320 ? -13.907 27.360  -1.611  1.00 37.90  ? 457 ASP   A N   1 
ATOM   2372 C  CA  . ASP   A 1 320 ? -12.947 28.188  -0.894  1.00 41.18  ? 457 ASP   A CA  1 
ATOM   2373 C  C   . ASP   A 1 320 ? -13.044 27.967  0.611   1.00 44.32  ? 457 ASP   A C   1 
ATOM   2374 O  O   . ASP   A 1 320 ? -14.122 27.729  1.164   1.00 41.76  ? 457 ASP   A O   1 
ATOM   2375 C  CB  . ASP   A 1 320 ? -13.162 29.669  -1.196  1.00 38.39  ? 457 ASP   A CB  1 
ATOM   2376 C  CG  . ASP   A 1 320 ? -12.445 30.125  -2.450  1.00 39.73  ? 457 ASP   A CG  1 
ATOM   2377 O  OD1 . ASP   A 1 320 ? -11.833 29.291  -3.153  1.00 38.05  ? 457 ASP   A OD1 1 
ATOM   2378 O  OD2 . ASP   A 1 320 ? -12.506 31.340  -2.744  1.00 43.23  ? 457 ASP   A OD2 1 
ATOM   2379 N  N   . GLY   A 1 321 ? -11.889 28.057  1.278   1.00 45.98  ? 458 GLY   A N   1 
ATOM   2380 C  CA  . GLY   A 1 321 ? -11.856 28.006  2.723   1.00 47.03  ? 458 GLY   A CA  1 
ATOM   2381 C  C   . GLY   A 1 321 ? -11.988 29.382  3.352   1.00 46.31  ? 458 GLY   A C   1 
ATOM   2382 O  O   . GLY   A 1 321 ? -11.923 30.411  2.680   1.00 44.60  ? 458 GLY   A O   1 
ATOM   2383 N  N   . GLY   A 1 322 ? -12.181 29.380  4.667   1.00 48.22  ? 459 GLY   A N   1 
ATOM   2384 C  CA  . GLY   A 1 322 ? -12.220 30.613  5.438   1.00 48.53  ? 459 GLY   A CA  1 
ATOM   2385 C  C   . GLY   A 1 322 ? -13.396 31.520  5.143   1.00 52.88  ? 459 GLY   A C   1 
ATOM   2386 O  O   . GLY   A 1 322 ? -13.229 32.744  5.092   1.00 53.11  ? 459 GLY   A O   1 
ATOM   2387 N  N   . ALA   A 1 323 ? -14.587 30.947  4.942   1.00 55.95  ? 460 ALA   A N   1 
ATOM   2388 C  CA  . ALA   A 1 323 ? -15.790 31.718  4.648   1.00 51.30  ? 460 ALA   A CA  1 
ATOM   2389 C  C   . ALA   A 1 323 ? -16.900 31.452  5.659   1.00 51.90  ? 460 ALA   A C   1 
ATOM   2390 O  O   . ALA   A 1 323 ? -18.060 31.785  5.401   1.00 47.27  ? 460 ALA   A O   1 
ATOM   2391 C  CB  . ALA   A 1 323 ? -16.290 31.427  3.232   1.00 47.47  ? 460 ALA   A CB  1 
ATOM   2392 N  N   . ASN   A 1 324 ? -16.563 30.860  6.807   1.00 53.51  ? 461 ASN   A N   1 
ATOM   2393 C  CA  . ASN   A 1 324 ? -17.572 30.491  7.794   1.00 56.72  ? 461 ASN   A CA  1 
ATOM   2394 C  C   . ASN   A 1 324 ? -18.136 31.711  8.513   1.00 53.29  ? 461 ASN   A C   1 
ATOM   2395 O  O   . ASN   A 1 324 ? -19.290 31.690  8.957   1.00 54.91  ? 461 ASN   A O   1 
ATOM   2396 C  CB  . ASN   A 1 324 ? -16.971 29.501  8.787   1.00 54.08  ? 461 ASN   A CB  1 
ATOM   2397 C  CG  . ASN   A 1 324 ? -16.136 28.437  8.106   1.00 59.92  ? 461 ASN   A CG  1 
ATOM   2398 O  OD1 . ASN   A 1 324 ? -16.656 27.416  7.657   1.00 60.33  ? 461 ASN   A OD1 1 
ATOM   2399 N  ND2 . ASN   A 1 324 ? -14.835 28.686  7.994   1.00 64.34  ? 461 ASN   A ND2 1 
ATOM   2400 N  N   . ASN   A 1 325 ? -17.358 32.789  8.612   1.00 53.09  ? 462 ASN   A N   1 
ATOM   2401 C  CA  . ASN   A 1 325 ? -17.843 34.048  9.160   1.00 51.45  ? 462 ASN   A CA  1 
ATOM   2402 C  C   . ASN   A 1 325 ? -18.321 35.013  8.083   1.00 51.03  ? 462 ASN   A C   1 
ATOM   2403 O  O   . ASN   A 1 325 ? -18.424 36.218  8.344   1.00 48.91  ? 462 ASN   A O   1 
ATOM   2404 C  CB  . ASN   A 1 325 ? -16.762 34.712  10.015  1.00 52.30  ? 462 ASN   A CB  1 
ATOM   2405 C  CG  . ASN   A 1 325 ? -16.420 33.903  11.259  1.00 58.16  ? 462 ASN   A CG  1 
ATOM   2406 O  OD1 . ASN   A 1 325 ? -17.080 32.909  11.558  1.00 61.80  ? 462 ASN   A OD1 1 
ATOM   2407 N  ND2 . ASN   A 1 325 ? -15.395 34.335  11.998  1.00 59.42  ? 462 ASN   A ND2 1 
ATOM   2408 N  N   . THR   A 1 326 ? -18.607 34.513  6.884   1.00 49.67  ? 463 THR   A N   1 
ATOM   2409 C  CA  . THR   A 1 326 ? -19.209 35.291  5.814   1.00 49.58  ? 463 THR   A CA  1 
ATOM   2410 C  C   . THR   A 1 326 ? -20.510 34.628  5.383   1.00 45.03  ? 463 THR   A C   1 
ATOM   2411 O  O   . THR   A 1 326 ? -20.856 33.533  5.832   1.00 44.86  ? 463 THR   A O   1 
ATOM   2412 C  CB  . THR   A 1 326 ? -18.264 35.431  4.612   1.00 51.68  ? 463 THR   A CB  1 
ATOM   2413 O  OG1 . THR   A 1 326 ? -18.390 34.281  3.766   1.00 48.70  ? 463 THR   A OG1 1 
ATOM   2414 C  CG2 . THR   A 1 326 ? -16.825 35.565  5.066   1.00 46.12  ? 463 THR   A CG2 1 
ATOM   2415 N  N   . SER   A 1 327 ? -21.235 35.316  4.501   1.00 43.20  ? 464 SER   A N   1 
ATOM   2416 C  CA  . SER   A 1 327 ? -22.528 34.857  4.012   1.00 46.02  ? 464 SER   A CA  1 
ATOM   2417 C  C   . SER   A 1 327 ? -22.423 34.117  2.683   1.00 46.93  ? 464 SER   A C   1 
ATOM   2418 O  O   . SER   A 1 327 ? -23.450 33.737  2.111   1.00 43.00  ? 464 SER   A O   1 
ATOM   2419 C  CB  . SER   A 1 327 ? -23.495 36.037  3.872   1.00 46.39  ? 464 SER   A CB  1 
ATOM   2420 O  OG  . SER   A 1 327 ? -22.823 37.206  3.434   1.00 48.79  ? 464 SER   A OG  1 
ATOM   2421 N  N   . ASN   A 1 328 ? -21.214 33.895  2.179   1.00 43.80  ? 465 ASN   A N   1 
ATOM   2422 C  CA  . ASN   A 1 328 ? -21.055 33.292  0.867   1.00 43.97  ? 465 ASN   A CA  1 
ATOM   2423 C  C   . ASN   A 1 328 ? -20.161 32.062  0.928   1.00 48.25  ? 465 ASN   A C   1 
ATOM   2424 O  O   . ASN   A 1 328 ? -19.313 31.911  1.811   1.00 47.42  ? 465 ASN   A O   1 
ATOM   2425 C  CB  . ASN   A 1 328 ? -20.478 34.281  -0.150  1.00 43.76  ? 465 ASN   A CB  1 
ATOM   2426 C  CG  . ASN   A 1 328 ? -20.999 35.683  0.038   1.00 47.95  ? 465 ASN   A CG  1 
ATOM   2427 O  OD1 . ASN   A 1 328 ? -22.110 36.006  -0.380  1.00 48.77  ? 465 ASN   A OD1 1 
ATOM   2428 N  ND2 . ASN   A 1 328 ? -20.187 36.536  0.643   1.00 49.43  ? 465 ASN   A ND2 1 
ATOM   2429 N  N   . GLU   A 1 329 ? -20.376 31.187  -0.050  1.00 43.30  ? 466 GLU   A N   1 
ATOM   2430 C  CA  . GLU   A 1 329 ? -19.500 30.066  -0.352  1.00 40.57  ? 466 GLU   A CA  1 
ATOM   2431 C  C   . GLU   A 1 329 ? -19.082 30.241  -1.804  1.00 41.20  ? 466 GLU   A C   1 
ATOM   2432 O  O   . GLU   A 1 329 ? -19.940 30.395  -2.679  1.00 40.07  ? 466 GLU   A O   1 
ATOM   2433 C  CB  . GLU   A 1 329 ? -20.225 28.732  -0.148  1.00 38.94  ? 466 GLU   A CB  1 
ATOM   2434 C  CG  . GLU   A 1 329 ? -20.610 28.438  1.296   1.00 42.02  ? 466 GLU   A CG  1 
ATOM   2435 C  CD  . GLU   A 1 329 ? -19.425 28.218  2.217   1.00 47.22  ? 466 GLU   A CD  1 
ATOM   2436 O  OE1 . GLU   A 1 329 ? -18.266 28.178  1.741   1.00 42.93  ? 466 GLU   A OE1 1 
ATOM   2437 O  OE2 . GLU   A 1 329 ? -19.659 28.100  3.439   1.00 47.16  ? 466 GLU   A OE2 1 
ATOM   2438 N  N   . THR   A 1 330 ? -17.781 30.273  -2.064  1.00 39.16  ? 467 THR   A N   1 
ATOM   2439 C  CA  . THR   A 1 330 ? -17.294 30.447  -3.424  1.00 40.28  ? 467 THR   A CA  1 
ATOM   2440 C  C   . THR   A 1 330 ? -16.695 29.139  -3.918  1.00 35.71  ? 467 THR   A C   1 
ATOM   2441 O  O   . THR   A 1 330 ? -15.967 28.461  -3.184  1.00 37.82  ? 467 THR   A O   1 
ATOM   2442 C  CB  . THR   A 1 330 ? -16.277 31.585  -3.522  1.00 39.14  ? 467 THR   A CB  1 
ATOM   2443 O  OG1 . THR   A 1 330 ? -14.995 31.116  -3.114  1.00 46.80  ? 467 THR   A OG1 1 
ATOM   2444 C  CG2 . THR   A 1 330 ? -16.681 32.731  -2.634  1.00 34.77  ? 467 THR   A CG2 1 
ATOM   2445 N  N   . PHE   A 1 331 ? -17.020 28.785  -5.157  1.00 34.69  ? 468 PHE   A N   1 
ATOM   2446 C  CA  . PHE   A 1 331 ? -16.642 27.514  -5.751  1.00 34.86  ? 468 PHE   A CA  1 
ATOM   2447 C  C   . PHE   A 1 331 ? -15.840 27.779  -7.012  1.00 31.26  ? 468 PHE   A C   1 
ATOM   2448 O  O   . PHE   A 1 331 ? -16.179 28.666  -7.798  1.00 36.04  ? 468 PHE   A O   1 
ATOM   2449 C  CB  . PHE   A 1 331 ? -17.874 26.670  -6.094  1.00 30.54  ? 468 PHE   A CB  1 
ATOM   2450 C  CG  . PHE   A 1 331 ? -18.645 26.211  -4.894  1.00 35.32  ? 468 PHE   A CG  1 
ATOM   2451 C  CD1 . PHE   A 1 331 ? -19.513 27.070  -4.242  1.00 34.46  ? 468 PHE   A CD1 1 
ATOM   2452 C  CD2 . PHE   A 1 331 ? -18.502 24.925  -4.417  1.00 34.66  ? 468 PHE   A CD2 1 
ATOM   2453 C  CE1 . PHE   A 1 331 ? -20.223 26.651  -3.125  1.00 34.87  ? 468 PHE   A CE1 1 
ATOM   2454 C  CE2 . PHE   A 1 331 ? -19.210 24.497  -3.304  1.00 41.12  ? 468 PHE   A CE2 1 
ATOM   2455 C  CZ  . PHE   A 1 331 ? -20.071 25.360  -2.657  1.00 35.78  ? 468 PHE   A CZ  1 
ATOM   2456 N  N   . ARG   A 1 332 ? -14.781 27.001  -7.202  1.00 31.03  ? 469 ARG   A N   1 
ATOM   2457 C  CA  . ARG   A 1 332 ? -13.886 27.165  -8.333  1.00 32.17  ? 469 ARG   A CA  1 
ATOM   2458 C  C   . ARG   A 1 332 ? -13.720 25.824  -9.032  1.00 28.01  ? 469 ARG   A C   1 
ATOM   2459 O  O   . ARG   A 1 332 ? -13.656 24.782  -8.365  1.00 27.38  ? 469 ARG   A O   1 
ATOM   2460 C  CB  . ARG   A 1 332 ? -12.524 27.698  -7.866  1.00 33.52  ? 469 ARG   A CB  1 
ATOM   2461 C  CG  . ARG   A 1 332 ? -12.596 29.110  -7.316  1.00 37.63  ? 469 ARG   A CG  1 
ATOM   2462 C  CD  . ARG   A 1 332 ? -11.315 29.512  -6.605  1.00 42.00  ? 469 ARG   A CD  1 
ATOM   2463 N  NE  . ARG   A 1 332 ? -11.553 30.621  -5.688  1.00 39.05  ? 469 ARG   A NE  1 
ATOM   2464 C  CZ  . ARG   A 1 332 ? -11.416 31.900  -6.009  1.00 41.86  ? 469 ARG   A CZ  1 
ATOM   2465 N  NH1 . ARG   A 1 332 ? -11.020 32.269  -7.216  1.00 42.96  ? 469 ARG   A NH1 1 
ATOM   2466 N  NH2 . ARG   A 1 332 ? -11.678 32.831  -5.096  1.00 45.35  ? 469 ARG   A NH2 1 
ATOM   2467 N  N   . PRO   A 1 333 ? -13.672 25.814  -10.363 1.00 29.37  ? 470 PRO   A N   1 
ATOM   2468 C  CA  . PRO   A 1 333 ? -13.494 24.546  -11.075 1.00 30.67  ? 470 PRO   A CA  1 
ATOM   2469 C  C   . PRO   A 1 333 ? -12.168 23.902  -10.699 1.00 31.75  ? 470 PRO   A C   1 
ATOM   2470 O  O   . PRO   A 1 333 ? -11.152 24.580  -10.523 1.00 33.24  ? 470 PRO   A O   1 
ATOM   2471 C  CB  . PRO   A 1 333 ? -13.543 24.953  -12.554 1.00 31.81  ? 470 PRO   A CB  1 
ATOM   2472 C  CG  . PRO   A 1 333 ? -13.236 26.406  -12.574 1.00 33.84  ? 470 PRO   A CG  1 
ATOM   2473 C  CD  . PRO   A 1 333 ? -13.727 26.968  -11.276 1.00 36.24  ? 470 PRO   A CD  1 
ATOM   2474 N  N   . GLY   A 1 334 ? -12.198 22.580  -10.544 1.00 31.51  ? 471 GLY   A N   1 
ATOM   2475 C  CA  . GLY   A 1 334 ? -11.025 21.849  -10.107 1.00 33.08  ? 471 GLY   A CA  1 
ATOM   2476 C  C   . GLY   A 1 334 ? -10.585 20.773  -11.072 1.00 31.83  ? 471 GLY   A C   1 
ATOM   2477 O  O   . GLY   A 1 334 ? -10.925 20.806  -12.256 1.00 29.68  ? 471 GLY   A O   1 
ATOM   2478 N  N   . GLY   A 1 335 ? -9.832  19.805  -10.572 1.00 31.87  ? 472 GLY   A N   1 
ATOM   2479 C  CA  . GLY   A 1 335 ? -9.342  18.708  -11.371 1.00 33.01  ? 472 GLY   A CA  1 
ATOM   2480 C  C   . GLY   A 1 335 ? -7.866  18.494  -11.164 1.00 31.45  ? 472 GLY   A C   1 
ATOM   2481 O  O   . GLY   A 1 335 ? -7.213  19.172  -10.375 1.00 34.21  ? 472 GLY   A O   1 
ATOM   2482 N  N   . GLY   A 1 336 ? -7.335  17.529  -11.906 1.00 32.12  ? 473 GLY   A N   1 
ATOM   2483 C  CA  . GLY   A 1 336 ? -5.945  17.152  -11.762 1.00 33.94  ? 473 GLY   A CA  1 
ATOM   2484 C  C   . GLY   A 1 336 ? -5.772  15.709  -11.337 1.00 33.93  ? 473 GLY   A C   1 
ATOM   2485 O  O   . GLY   A 1 336 ? -4.900  14.999  -11.848 1.00 35.49  ? 473 GLY   A O   1 
ATOM   2486 N  N   . ASP   A 1 337 ? -6.599  15.267  -10.391 1.00 33.62  ? 474 ASP   A N   1 
ATOM   2487 C  CA  . ASP   A 1 337 ? -6.610  13.876  -9.941  1.00 31.51  ? 474 ASP   A CA  1 
ATOM   2488 C  C   . ASP   A 1 337 ? -7.648  13.137  -10.773 1.00 29.52  ? 474 ASP   A C   1 
ATOM   2489 O  O   . ASP   A 1 337 ? -8.849  13.238  -10.515 1.00 30.92  ? 474 ASP   A O   1 
ATOM   2490 C  CB  . ASP   A 1 337 ? -6.931  13.790  -8.454  1.00 33.17  ? 474 ASP   A CB  1 
ATOM   2491 C  CG  . ASP   A 1 337 ? -6.864  12.362  -7.914  1.00 33.62  ? 474 ASP   A CG  1 
ATOM   2492 O  OD1 . ASP   A 1 337 ? -6.668  11.412  -8.705  1.00 30.88  ? 474 ASP   A OD1 1 
ATOM   2493 O  OD2 . ASP   A 1 337 ? -7.005  12.189  -6.682  1.00 33.74  ? 474 ASP   A OD2 1 
ATOM   2494 N  N   . MET   A 1 338 ? -7.187  12.390  -11.781 1.00 29.36  ? 475 MET   A N   1 
ATOM   2495 C  CA  . MET   A 1 338 ? -8.123  11.718  -12.673 1.00 31.37  ? 475 MET   A CA  1 
ATOM   2496 C  C   . MET   A 1 338 ? -8.890  10.601  -11.982 1.00 28.57  ? 475 MET   A C   1 
ATOM   2497 O  O   . MET   A 1 338 ? -9.865  10.104  -12.559 1.00 28.42  ? 475 MET   A O   1 
ATOM   2498 C  CB  . MET   A 1 338 ? -7.408  11.142  -13.893 1.00 29.23  ? 475 MET   A CB  1 
ATOM   2499 C  CG  . MET   A 1 338 ? -6.942  12.182  -14.894 1.00 34.07  ? 475 MET   A CG  1 
ATOM   2500 S  SD  . MET   A 1 338 ? -8.118  13.497  -15.289 1.00 30.11  ? 475 MET   A SD  1 
ATOM   2501 C  CE  . MET   A 1 338 ? -7.007  14.892  -15.298 1.00 31.00  ? 475 MET   A CE  1 
ATOM   2502 N  N   . ARG   A 1 339 ? -8.464  10.178  -10.787 1.00 29.56  ? 476 ARG   A N   1 
ATOM   2503 C  CA  . ARG   A 1 339 ? -9.248  9.201   -10.040 1.00 31.72  ? 476 ARG   A CA  1 
ATOM   2504 C  C   . ARG   A 1 339 ? -10.664 9.709   -9.804  1.00 28.91  ? 476 ARG   A C   1 
ATOM   2505 O  O   . ARG   A 1 339 ? -11.622 8.927   -9.819  1.00 31.44  ? 476 ARG   A O   1 
ATOM   2506 C  CB  . ARG   A 1 339 ? -8.560  8.868   -8.719  1.00 32.55  ? 476 ARG   A CB  1 
ATOM   2507 C  CG  . ARG   A 1 339 ? -7.272  8.065   -8.875  1.00 36.27  ? 476 ARG   A CG  1 
ATOM   2508 C  CD  . ARG   A 1 339 ? -6.585  7.869   -7.540  1.00 35.20  ? 476 ARG   A CD  1 
ATOM   2509 N  NE  . ARG   A 1 339 ? -6.367  9.149   -6.881  1.00 39.92  ? 476 ARG   A NE  1 
ATOM   2510 C  CZ  . ARG   A 1 339 ? -6.123  9.297   -5.585  1.00 43.89  ? 476 ARG   A CZ  1 
ATOM   2511 N  NH1 . ARG   A 1 339 ? -6.053  8.256   -4.768  1.00 51.74  ? 476 ARG   A NH1 1 
ATOM   2512 N  NH2 . ARG   A 1 339 ? -5.938  10.519  -5.096  1.00 42.77  ? 476 ARG   A NH2 1 
ATOM   2513 N  N   . ASP   A 1 340 ? -10.815 11.023  -9.603  1.00 32.58  ? 477 ASP   A N   1 
ATOM   2514 C  CA  . ASP   A 1 340 ? -12.140 11.612  -9.453  1.00 30.20  ? 477 ASP   A CA  1 
ATOM   2515 C  C   . ASP   A 1 340 ? -12.945 11.513  -10.740 1.00 29.88  ? 477 ASP   A C   1 
ATOM   2516 O  O   . ASP   A 1 340 ? -14.178 11.428  -10.688 1.00 30.76  ? 477 ASP   A O   1 
ATOM   2517 C  CB  . ASP   A 1 340 ? -12.022 13.063  -9.005  1.00 33.58  ? 477 ASP   A CB  1 
ATOM   2518 C  CG  . ASP   A 1 340 ? -11.383 13.192  -7.644  1.00 35.67  ? 477 ASP   A CG  1 
ATOM   2519 O  OD1 . ASP   A 1 340 ? -11.400 12.197  -6.890  1.00 39.02  ? 477 ASP   A OD1 1 
ATOM   2520 O  OD2 . ASP   A 1 340 ? -10.857 14.285  -7.331  1.00 36.46  ? 477 ASP   A OD2 1 
ATOM   2521 N  N   . ASN   A 1 341 ? -12.274 11.512  -11.896 1.00 32.97  ? 478 ASN   A N   1 
ATOM   2522 C  CA  . ASN   A 1 341 ? -12.981 11.276  -13.152 1.00 30.28  ? 478 ASN   A CA  1 
ATOM   2523 C  C   . ASN   A 1 341 ? -13.553 9.863   -13.200 1.00 26.24  ? 478 ASN   A C   1 
ATOM   2524 O  O   . ASN   A 1 341 ? -14.752 9.676   -13.442 1.00 28.03  ? 478 ASN   A O   1 
ATOM   2525 C  CB  . ASN   A 1 341 ? -12.062 11.545  -14.344 1.00 28.94  ? 478 ASN   A CB  1 
ATOM   2526 C  CG  . ASN   A 1 341 ? -11.682 13.007  -14.474 1.00 33.32  ? 478 ASN   A CG  1 
ATOM   2527 O  OD1 . ASN   A 1 341 ? -11.492 13.710  -13.481 1.00 33.69  ? 478 ASN   A OD1 1 
ATOM   2528 N  ND2 . ASN   A 1 341 ? -11.577 13.477  -15.715 1.00 25.21  ? 478 ASN   A ND2 1 
ATOM   2529 N  N   . TRP   A 1 342 ? -12.710 8.849   -12.959 1.00 30.71  ? 479 TRP   A N   1 
ATOM   2530 C  CA  . TRP   A 1 342 ? -13.208 7.475   -12.918 1.00 29.34  ? 479 TRP   A CA  1 
ATOM   2531 C  C   . TRP   A 1 342 ? -14.216 7.301   -11.796 1.00 28.79  ? 479 TRP   A C   1 
ATOM   2532 O  O   . TRP   A 1 342 ? -15.177 6.529   -11.925 1.00 29.61  ? 479 TRP   A O   1 
ATOM   2533 C  CB  . TRP   A 1 342 ? -12.062 6.483   -12.724 1.00 25.48  ? 479 TRP   A CB  1 
ATOM   2534 C  CG  . TRP   A 1 342 ? -10.752 6.903   -13.298 1.00 25.43  ? 479 TRP   A CG  1 
ATOM   2535 C  CD1 . TRP   A 1 342 ? -9.532  6.785   -12.700 1.00 23.20  ? 479 TRP   A CD1 1 
ATOM   2536 C  CD2 . TRP   A 1 342 ? -10.516 7.508   -14.577 1.00 28.89  ? 479 TRP   A CD2 1 
ATOM   2537 N  NE1 . TRP   A 1 342 ? -8.552  7.272   -13.525 1.00 25.10  ? 479 TRP   A NE1 1 
ATOM   2538 C  CE2 . TRP   A 1 342 ? -9.130  7.726   -14.682 1.00 26.08  ? 479 TRP   A CE2 1 
ATOM   2539 C  CE3 . TRP   A 1 342 ? -11.341 7.886   -15.643 1.00 24.93  ? 479 TRP   A CE3 1 
ATOM   2540 C  CZ2 . TRP   A 1 342 ? -8.550  8.300   -15.805 1.00 24.24  ? 479 TRP   A CZ2 1 
ATOM   2541 C  CZ3 . TRP   A 1 342 ? -10.765 8.461   -16.753 1.00 26.55  ? 479 TRP   A CZ3 1 
ATOM   2542 C  CH2 . TRP   A 1 342 ? -9.380  8.661   -16.829 1.00 25.27  ? 479 TRP   A CH2 1 
ATOM   2543 N  N   . ARG   A 1 343 ? -13.992 8.012   -10.691 1.00 31.07  ? 480 ARG   A N   1 
ATOM   2544 C  CA  . ARG   A 1 343 ? -14.868 7.952   -9.533  1.00 30.34  ? 480 ARG   A CA  1 
ATOM   2545 C  C   . ARG   A 1 343 ? -16.269 8.417   -9.898  1.00 31.19  ? 480 ARG   A C   1 
ATOM   2546 O  O   . ARG   A 1 343 ? -17.260 7.917   -9.354  1.00 28.83  ? 480 ARG   A O   1 
ATOM   2547 C  CB  . ARG   A 1 343 ? -14.277 8.846   -8.459  1.00 36.60  ? 480 ARG   A CB  1 
ATOM   2548 C  CG  . ARG   A 1 343 ? -14.679 8.597   -7.072  1.00 39.15  ? 480 ARG   A CG  1 
ATOM   2549 C  CD  . ARG   A 1 343 ? -14.115 9.737   -6.269  1.00 35.53  ? 480 ARG   A CD  1 
ATOM   2550 N  NE  . ARG   A 1 343 ? -12.662 9.744   -6.120  1.00 37.35  ? 480 ARG   A NE  1 
ATOM   2551 C  CZ  . ARG   A 1 343 ? -11.917 8.734   -5.690  1.00 36.22  ? 480 ARG   A CZ  1 
ATOM   2552 N  NH1 . ARG   A 1 343 ? -12.453 7.597   -5.273  1.00 38.17  ? 480 ARG   A NH1 1 
ATOM   2553 N  NH2 . ARG   A 1 343 ? -10.597 8.882   -5.641  1.00 36.29  ? 480 ARG   A NH2 1 
ATOM   2554 N  N   . SER   A 1 344 ? -16.365 9.379   -10.821 1.00 32.09  ? 481 SER   A N   1 
ATOM   2555 C  CA  . SER   A 1 344 ? -17.645 9.950   -11.220 1.00 31.90  ? 481 SER   A CA  1 
ATOM   2556 C  C   . SER   A 1 344 ? -18.536 8.942   -11.931 1.00 31.37  ? 481 SER   A C   1 
ATOM   2557 O  O   . SER   A 1 344 ? -19.747 9.165   -12.033 1.00 33.55  ? 481 SER   A O   1 
ATOM   2558 C  CB  . SER   A 1 344 ? -17.411 11.155  -12.125 1.00 33.81  ? 481 SER   A CB  1 
ATOM   2559 O  OG  . SER   A 1 344 ? -16.962 10.735  -13.404 1.00 30.78  ? 481 SER   A OG  1 
ATOM   2560 N  N   . GLU   A 1 345 ? -17.965 7.851   -12.433 1.00 32.44  ? 482 GLU   A N   1 
ATOM   2561 C  CA  . GLU   A 1 345 ? -18.709 6.801   -13.109 1.00 33.22  ? 482 GLU   A CA  1 
ATOM   2562 C  C   . GLU   A 1 345 ? -18.709 5.489   -12.341 1.00 31.50  ? 482 GLU   A C   1 
ATOM   2563 O  O   . GLU   A 1 345 ? -19.650 4.701   -12.476 1.00 34.40  ? 482 GLU   A O   1 
ATOM   2564 C  CB  . GLU   A 1 345 ? -18.116 6.549   -14.502 1.00 32.46  ? 482 GLU   A CB  1 
ATOM   2565 C  CG  . GLU   A 1 345 ? -18.205 7.732   -15.461 1.00 32.39  ? 482 GLU   A CG  1 
ATOM   2566 C  CD  . GLU   A 1 345 ? -19.614 8.249   -15.655 1.00 32.18  ? 482 GLU   A CD  1 
ATOM   2567 O  OE1 . GLU   A 1 345 ? -20.560 7.431   -15.654 1.00 39.47  ? 482 GLU   A OE1 1 
ATOM   2568 O  OE2 . GLU   A 1 345 ? -19.778 9.476   -15.831 1.00 34.47  ? 482 GLU   A OE2 1 
ATOM   2569 N  N   . LEU   A 1 346 ? -17.679 5.242   -11.538 1.00 31.12  ? 483 LEU   A N   1 
ATOM   2570 C  CA  . LEU   A 1 346 ? -17.520 4.023   -10.758 1.00 30.50  ? 483 LEU   A CA  1 
ATOM   2571 C  C   . LEU   A 1 346 ? -18.233 4.096   -9.416  1.00 30.69  ? 483 LEU   A C   1 
ATOM   2572 O  O   . LEU   A 1 346 ? -18.247 3.104   -8.678  1.00 35.34  ? 483 LEU   A O   1 
ATOM   2573 C  CB  . LEU   A 1 346 ? -16.027 3.757   -10.531 1.00 26.88  ? 483 LEU   A CB  1 
ATOM   2574 C  CG  . LEU   A 1 346 ? -15.276 3.091   -11.685 1.00 30.42  ? 483 LEU   A CG  1 
ATOM   2575 C  CD1 . LEU   A 1 346 ? -13.778 3.050   -11.402 1.00 31.51  ? 483 LEU   A CD1 1 
ATOM   2576 C  CD2 . LEU   A 1 346 ? -15.812 1.696   -11.948 1.00 30.03  ? 483 LEU   A CD2 1 
ATOM   2577 N  N   . TYR   A 1 347 ? -18.819 5.251   -9.096  1.00 33.69  ? 484 TYR   A N   1 
ATOM   2578 C  CA  . TYR   A 1 347 ? -19.360 5.511   -7.767  1.00 30.39  ? 484 TYR   A CA  1 
ATOM   2579 C  C   . TYR   A 1 347 ? -20.418 4.505   -7.334  1.00 31.34  ? 484 TYR   A C   1 
ATOM   2580 O  O   . TYR   A 1 347 ? -20.585 4.276   -6.131  1.00 35.77  ? 484 TYR   A O   1 
ATOM   2581 C  CB  . TYR   A 1 347 ? -19.912 6.937   -7.719  1.00 35.02  ? 484 TYR   A CB  1 
ATOM   2582 C  CG  . TYR   A 1 347 ? -21.191 7.122   -8.497  1.00 37.52  ? 484 TYR   A CG  1 
ATOM   2583 C  CD1 . TYR   A 1 347 ? -21.147 7.308   -9.869  1.00 30.65  ? 484 TYR   A CD1 1 
ATOM   2584 C  CD2 . TYR   A 1 347 ? -22.434 7.064   -7.881  1.00 32.92  ? 484 TYR   A CD2 1 
ATOM   2585 C  CE1 . TYR   A 1 347 ? -22.290 7.469   -10.609 1.00 32.10  ? 484 TYR   A CE1 1 
ATOM   2586 C  CE2 . TYR   A 1 347 ? -23.594 7.217   -8.617  1.00 33.93  ? 484 TYR   A CE2 1 
ATOM   2587 C  CZ  . TYR   A 1 347 ? -23.514 7.420   -9.982  1.00 35.95  ? 484 TYR   A CZ  1 
ATOM   2588 O  OH  . TYR   A 1 347 ? -24.663 7.578   -10.725 1.00 41.05  ? 484 TYR   A OH  1 
ATOM   2589 N  N   . LYS   A 1 348 ? -21.152 3.906   -8.266  1.00 33.09  ? 485 LYS   A N   1 
ATOM   2590 C  CA  . LYS   A 1 348 ? -22.229 3.010   -7.863  1.00 37.27  ? 485 LYS   A CA  1 
ATOM   2591 C  C   . LYS   A 1 348 ? -21.806 1.546   -7.809  1.00 36.98  ? 485 LYS   A C   1 
ATOM   2592 O  O   . LYS   A 1 348 ? -22.659 0.680   -7.597  1.00 38.20  ? 485 LYS   A O   1 
ATOM   2593 C  CB  . LYS   A 1 348 ? -23.448 3.182   -8.774  1.00 37.27  ? 485 LYS   A CB  1 
ATOM   2594 C  CG  . LYS   A 1 348 ? -23.275 2.838   -10.240 1.00 37.01  ? 485 LYS   A CG  1 
ATOM   2595 C  CD  . LYS   A 1 348 ? -24.498 3.357   -10.997 1.00 42.42  ? 485 LYS   A CD  1 
ATOM   2596 C  CE  . LYS   A 1 348 ? -24.580 2.841   -12.418 1.00 47.52  ? 485 LYS   A CE  1 
ATOM   2597 N  NZ  . LYS   A 1 348 ? -25.858 3.269   -13.063 1.00 48.96  ? 485 LYS   A NZ  1 
ATOM   2598 N  N   . TYR   A 1 349 ? -20.516 1.251   -7.957  1.00 37.44  ? 486 TYR   A N   1 
ATOM   2599 C  CA  . TYR   A 1 349 ? -20.011 -0.112  -7.894  1.00 33.56  ? 486 TYR   A CA  1 
ATOM   2600 C  C   . TYR   A 1 349 ? -19.089 -0.299  -6.694  1.00 38.48  ? 486 TYR   A C   1 
ATOM   2601 O  O   . TYR   A 1 349 ? -18.465 0.650   -6.211  1.00 39.54  ? 486 TYR   A O   1 
ATOM   2602 C  CB  . TYR   A 1 349 ? -19.251 -0.488  -9.170  1.00 36.94  ? 486 TYR   A CB  1 
ATOM   2603 C  CG  . TYR   A 1 349 ? -20.043 -0.368  -10.449 1.00 33.51  ? 486 TYR   A CG  1 
ATOM   2604 C  CD1 . TYR   A 1 349 ? -20.999 -1.313  -10.788 1.00 36.49  ? 486 TYR   A CD1 1 
ATOM   2605 C  CD2 . TYR   A 1 349 ? -19.814 0.676   -11.332 1.00 34.37  ? 486 TYR   A CD2 1 
ATOM   2606 C  CE1 . TYR   A 1 349 ? -21.719 -1.215  -11.964 1.00 35.15  ? 486 TYR   A CE1 1 
ATOM   2607 C  CE2 . TYR   A 1 349 ? -20.525 0.784   -12.512 1.00 32.03  ? 486 TYR   A CE2 1 
ATOM   2608 C  CZ  . TYR   A 1 349 ? -21.477 -0.163  -12.822 1.00 37.55  ? 486 TYR   A CZ  1 
ATOM   2609 O  OH  . TYR   A 1 349 ? -22.187 -0.055  -13.999 1.00 39.59  ? 486 TYR   A OH  1 
ATOM   2610 N  N   . LYS   A 1 350 ? -18.999 -1.547  -6.233  1.00 37.45  ? 487 LYS   A N   1 
ATOM   2611 C  CA  . LYS   A 1 350 ? -18.105 -1.932  -5.149  1.00 38.74  ? 487 LYS   A CA  1 
ATOM   2612 C  C   . LYS   A 1 350 ? -17.954 -3.449  -5.160  1.00 41.36  ? 487 LYS   A C   1 
ATOM   2613 O  O   . LYS   A 1 350 ? -18.928 -4.178  -5.372  1.00 39.97  ? 487 LYS   A O   1 
ATOM   2614 C  CB  . LYS   A 1 350 ? -18.611 -1.410  -3.798  1.00 38.02  ? 487 LYS   A CB  1 
ATOM   2615 C  CG  . LYS   A 1 350 ? -19.477 -2.358  -2.984  1.00 43.74  ? 487 LYS   A CG  1 
ATOM   2616 C  CD  . LYS   A 1 350 ? -19.480 -1.979  -1.511  1.00 43.94  ? 487 LYS   A CD  1 
ATOM   2617 C  CE  . LYS   A 1 350 ? -19.932 -3.149  -0.659  1.00 49.39  ? 487 LYS   A CE  1 
ATOM   2618 N  NZ  . LYS   A 1 350 ? -19.956 -2.825  0.806   1.00 51.81  ? 487 LYS   A NZ  1 
ATOM   2619 N  N   . VAL   A 1 351 ? -16.715 -3.911  -4.984  1.00 39.80  ? 488 VAL   A N   1 
ATOM   2620 C  CA  . VAL   A 1 351 ? -16.370 -5.324  -5.104  1.00 41.78  ? 488 VAL   A CA  1 
ATOM   2621 C  C   . VAL   A 1 351 ? -16.585 -6.017  -3.771  1.00 41.46  ? 488 VAL   A C   1 
ATOM   2622 O  O   . VAL   A 1 351 ? -16.205 -5.500  -2.716  1.00 40.69  ? 488 VAL   A O   1 
ATOM   2623 C  CB  . VAL   A 1 351 ? -14.917 -5.496  -5.588  1.00 42.63  ? 488 VAL   A CB  1 
ATOM   2624 C  CG1 . VAL   A 1 351 ? -14.542 -6.976  -5.639  1.00 42.68  ? 488 VAL   A CG1 1 
ATOM   2625 C  CG2 . VAL   A 1 351 ? -14.743 -4.876  -6.957  1.00 38.51  ? 488 VAL   A CG2 1 
ATOM   2626 N  N   . VAL   A 1 352 ? -17.189 -7.202  -3.822  1.00 42.98  ? 489 VAL   A N   1 
ATOM   2627 C  CA  . VAL   A 1 352 ? -17.381 -8.035  -2.646  1.00 44.65  ? 489 VAL   A CA  1 
ATOM   2628 C  C   . VAL   A 1 352 ? -16.901 -9.446  -2.968  1.00 46.08  ? 489 VAL   A C   1 
ATOM   2629 O  O   . VAL   A 1 352 ? -16.851 -9.869  -4.127  1.00 42.16  ? 489 VAL   A O   1 
ATOM   2630 C  CB  . VAL   A 1 352 ? -18.848 -8.053  -2.171  1.00 42.43  ? 489 VAL   A CB  1 
ATOM   2631 C  CG1 . VAL   A 1 352 ? -19.341 -6.636  -1.913  1.00 43.50  ? 489 VAL   A CG1 1 
ATOM   2632 C  CG2 . VAL   A 1 352 ? -19.728 -8.732  -3.196  1.00 44.09  ? 489 VAL   A CG2 1 
ATOM   2633 N  N   . GLN   A 1 353 ? -16.531 -10.173 -1.920  1.00 43.70  ? 490 GLN   A N   1 
ATOM   2634 C  CA  . GLN   A 1 353 ? -16.116 -11.562 -2.044  1.00 49.71  ? 490 GLN   A CA  1 
ATOM   2635 C  C   . GLN   A 1 353 ? -17.271 -12.485 -1.688  1.00 50.36  ? 490 GLN   A C   1 
ATOM   2636 O  O   . GLN   A 1 353 ? -18.046 -12.202 -0.776  1.00 52.49  ? 490 GLN   A O   1 
ATOM   2637 C  CB  . GLN   A 1 353 ? -14.930 -11.852 -1.120  1.00 51.07  ? 490 GLN   A CB  1 
ATOM   2638 C  CG  . GLN   A 1 353 ? -14.609 -13.317 -0.974  1.00 53.59  ? 490 GLN   A CG  1 
ATOM   2639 C  CD  . GLN   A 1 353 ? -13.195 -13.536 -0.503  1.00 51.27  ? 490 GLN   A CD  1 
ATOM   2640 O  OE1 . GLN   A 1 353 ? -12.591 -12.665 0.131   1.00 55.89  ? 490 GLN   A OE1 1 
ATOM   2641 N  NE2 . GLN   A 1 353 ? -12.634 -14.680 -0.858  1.00 53.35  ? 490 GLN   A NE2 1 
ATOM   2642 N  N   . ILE   A 1 354 ? -17.401 -13.574 -2.439  1.00 49.10  ? 491 ILE   A N   1 
ATOM   2643 C  CA  . ILE   A 1 354 ? -18.427 -14.560 -2.130  1.00 54.27  ? 491 ILE   A CA  1 
ATOM   2644 C  C   . ILE   A 1 354 ? -17.915 -15.356 -0.929  1.00 58.38  ? 491 ILE   A C   1 
ATOM   2645 O  O   . ILE   A 1 354 ? -17.045 -16.215 -1.070  1.00 60.13  ? 491 ILE   A O   1 
ATOM   2646 C  CB  . ILE   A 1 354 ? -18.760 -15.449 -3.334  1.00 55.41  ? 491 ILE   A CB  1 
ATOM   2647 C  CG1 . ILE   A 1 354 ? -19.658 -14.694 -4.298  1.00 53.20  ? 491 ILE   A CG1 1 
ATOM   2648 C  CG2 . ILE   A 1 354 ? -19.533 -16.669 -2.926  1.00 57.77  ? 491 ILE   A CG2 1 
ATOM   2649 C  CD1 . ILE   A 1 354 ? -20.773 -13.911 -3.605  1.00 52.36  ? 491 ILE   A CD1 1 
ATOM   2650 N  N   . GLU   A 1 355 ? -18.442 -15.058 0.265   1.00 58.05  ? 492 GLU   A N   1 
ATOM   2651 C  CA  . GLU   A 1 355 ? -18.042 -15.737 1.498   1.00 59.27  ? 492 GLU   A CA  1 
ATOM   2652 C  C   . GLU   A 1 355 ? -18.688 -17.111 1.573   1.00 63.23  ? 492 GLU   A C   1 
ATOM   2653 O  O   . GLU   A 1 355 ? -18.743 -17.699 2.653   1.00 65.29  ? 492 GLU   A O   1 
ATOM   2654 C  CB  . GLU   A 1 355 ? -18.432 -14.911 2.733   1.00 59.91  ? 492 GLU   A CB  1 
ATOM   2655 C  CG  . GLU   A 1 355 ? -17.344 -14.010 3.276   1.00 61.68  ? 492 GLU   A CG  1 
ATOM   2656 C  CD  . GLU   A 1 355 ? -17.196 -14.126 4.785   1.00 64.13  ? 492 GLU   A CD  1 
ATOM   2657 O  OE1 . GLU   A 1 355 ? -18.166 -13.836 5.518   1.00 64.52  ? 492 GLU   A OE1 1 
ATOM   2658 O  OE2 . GLU   A 1 355 ? -16.101 -14.509 5.248   1.00 65.06  ? 492 GLU   A OE2 1 
ATOM   2659 O  OXT . GLU   A 1 355 ? -19.187 -17.649 0.581   1.00 66.04  ? 492 GLU   A OXT 1 
HETATM 2660 C  C1  . NAG   B 2 .   ? -24.741 11.263  1.141   1.00 47.82  ? 501 NAG   A C1  1 
HETATM 2661 C  C2  . NAG   B 2 .   ? -24.327 12.458  1.986   1.00 43.28  ? 501 NAG   A C2  1 
HETATM 2662 C  C3  . NAG   B 2 .   ? -23.911 11.992  3.376   1.00 43.19  ? 501 NAG   A C3  1 
HETATM 2663 C  C4  . NAG   B 2 .   ? -25.024 11.165  4.009   1.00 50.05  ? 501 NAG   A C4  1 
HETATM 2664 C  C5  . NAG   B 2 .   ? -25.470 10.043  3.070   1.00 51.15  ? 501 NAG   A C5  1 
HETATM 2665 C  C6  . NAG   B 2 .   ? -26.689 9.306   3.572   1.00 53.39  ? 501 NAG   A C6  1 
HETATM 2666 C  C7  . NAG   B 2 .   ? -23.458 14.327  0.654   1.00 46.22  ? 501 NAG   A C7  1 
HETATM 2667 C  C8  . NAG   B 2 .   ? -22.239 14.964  0.060   1.00 44.44  ? 501 NAG   A C8  1 
HETATM 2668 N  N2  . NAG   B 2 .   ? -23.253 13.202  1.349   1.00 45.35  ? 501 NAG   A N2  1 
HETATM 2669 O  O3  . NAG   B 2 .   ? -23.625 13.125  4.187   1.00 46.15  ? 501 NAG   A O3  1 
HETATM 2670 O  O4  . NAG   B 2 .   ? -24.565 10.595  5.229   1.00 52.25  ? 501 NAG   A O4  1 
HETATM 2671 O  O5  . NAG   B 2 .   ? -25.815 10.574  1.781   1.00 47.65  ? 501 NAG   A O5  1 
HETATM 2672 O  O6  . NAG   B 2 .   ? -26.346 8.350   4.565   1.00 68.02  ? 501 NAG   A O6  1 
HETATM 2673 O  O7  . NAG   B 2 .   ? -24.579 14.807  0.512   1.00 46.87  ? 501 NAG   A O7  1 
HETATM 2674 C  C1  . NAG   C 2 .   ? -34.168 -0.659  -8.406  1.00 66.29  ? 502 NAG   A C1  1 
HETATM 2675 C  C2  . NAG   C 2 .   ? -35.554 -0.048  -8.680  1.00 71.71  ? 502 NAG   A C2  1 
HETATM 2676 C  C3  . NAG   C 2 .   ? -35.660 0.521   -10.108 1.00 72.94  ? 502 NAG   A C3  1 
HETATM 2677 C  C4  . NAG   C 2 .   ? -35.110 -0.427  -11.172 1.00 70.55  ? 502 NAG   A C4  1 
HETATM 2678 C  C5  . NAG   C 2 .   ? -33.919 -1.219  -10.651 1.00 66.36  ? 502 NAG   A C5  1 
HETATM 2679 C  C6  . NAG   C 2 .   ? -32.814 -1.380  -11.668 1.00 66.09  ? 502 NAG   A C6  1 
HETATM 2680 C  C7  . NAG   C 2 .   ? -36.923 -1.443  -7.195  1.00 77.03  ? 502 NAG   A C7  1 
HETATM 2681 C  C8  . NAG   C 2 .   ? -38.043 -2.436  -7.111  1.00 76.13  ? 502 NAG   A C8  1 
HETATM 2682 N  N2  . NAG   C 2 .   ? -36.613 -1.011  -8.424  1.00 75.32  ? 502 NAG   A N2  1 
HETATM 2683 O  O3  . NAG   C 2 .   ? -34.992 1.776   -10.173 1.00 77.87  ? 502 NAG   A O3  1 
HETATM 2684 O  O4  . NAG   C 2 .   ? -36.125 -1.324  -11.610 1.00 76.50  ? 502 NAG   A O4  1 
HETATM 2685 O  O5  . NAG   C 2 .   ? -33.358 -0.522  -9.536  1.00 64.29  ? 502 NAG   A O5  1 
HETATM 2686 O  O6  . NAG   C 2 .   ? -31.829 -2.298  -11.215 1.00 63.41  ? 502 NAG   A O6  1 
HETATM 2687 O  O7  . NAG   C 2 .   ? -36.327 -1.049  -6.196  1.00 75.87  ? 502 NAG   A O7  1 
HETATM 2688 C  C1  . NAG   D 2 .   ? -16.963 12.700  -26.652 1.00 32.09  ? 503 NAG   A C1  1 
HETATM 2689 C  C2  . NAG   D 2 .   ? -15.572 12.920  -27.245 1.00 31.14  ? 503 NAG   A C2  1 
HETATM 2690 C  C3  . NAG   D 2 .   ? -15.686 13.370  -28.698 1.00 32.57  ? 503 NAG   A C3  1 
HETATM 2691 C  C4  . NAG   D 2 .   ? -16.522 12.379  -29.495 1.00 35.59  ? 503 NAG   A C4  1 
HETATM 2692 C  C5  . NAG   D 2 .   ? -17.882 12.198  -28.832 1.00 36.17  ? 503 NAG   A C5  1 
HETATM 2693 C  C6  . NAG   D 2 .   ? -18.728 11.140  -29.502 1.00 34.85  ? 503 NAG   A C6  1 
HETATM 2694 C  C7  . NAG   D 2 .   ? -13.693 13.593  -25.814 1.00 33.69  ? 503 NAG   A C7  1 
HETATM 2695 C  C8  . NAG   D 2 .   ? -13.046 14.724  -25.071 1.00 29.30  ? 503 NAG   A C8  1 
HETATM 2696 N  N2  . NAG   D 2 .   ? -14.819 13.892  -26.470 1.00 29.11  ? 503 NAG   A N2  1 
HETATM 2697 O  O3  . NAG   D 2 .   ? -14.386 13.481  -29.264 1.00 33.29  ? 503 NAG   A O3  1 
HETATM 2698 O  O4  . NAG   D 2 .   ? -16.711 12.852  -30.824 1.00 41.52  ? 503 NAG   A O4  1 
HETATM 2699 O  O5  . NAG   D 2 .   ? -17.700 11.779  -27.473 1.00 28.41  ? 503 NAG   A O5  1 
HETATM 2700 O  O6  . NAG   D 2 .   ? -18.219 9.836   -29.251 1.00 45.85  ? 503 NAG   A O6  1 
HETATM 2701 O  O7  . NAG   D 2 .   ? -13.218 12.461  -25.820 1.00 24.38  ? 503 NAG   A O7  1 
HETATM 2702 C  C1  . NAG   E 2 .   ? -15.513 16.770  7.713   1.00 54.82  ? 504 NAG   A C1  1 
HETATM 2703 C  C2  . NAG   E 2 .   ? -15.163 15.895  8.913   1.00 58.67  ? 504 NAG   A C2  1 
HETATM 2704 C  C3  . NAG   E 2 .   ? -15.112 16.737  10.183  1.00 61.24  ? 504 NAG   A C3  1 
HETATM 2705 C  C4  . NAG   E 2 .   ? -14.166 17.915  9.998   1.00 59.66  ? 504 NAG   A C4  1 
HETATM 2706 C  C5  . NAG   E 2 .   ? -14.562 18.714  8.761   1.00 52.81  ? 504 NAG   A C5  1 
HETATM 2707 C  C6  . NAG   E 2 .   ? -13.584 19.816  8.429   1.00 54.61  ? 504 NAG   A C6  1 
HETATM 2708 C  C7  . NAG   E 2 .   ? -15.750 13.521  9.131   1.00 56.73  ? 504 NAG   A C7  1 
HETATM 2709 C  C8  . NAG   E 2 .   ? -16.864 12.529  9.277   1.00 57.88  ? 504 NAG   A C8  1 
HETATM 2710 N  N2  . NAG   E 2 .   ? -16.114 14.805  9.058   1.00 57.47  ? 504 NAG   A N2  1 
HETATM 2711 O  O3  . NAG   E 2 .   ? -14.677 15.924  11.268  1.00 66.64  ? 504 NAG   A O3  1 
HETATM 2712 O  O4  . NAG   E 2 .   ? -14.212 18.763  11.140  1.00 69.39  ? 504 NAG   A O4  1 
HETATM 2713 O  O5  . NAG   E 2 .   ? -14.591 17.848  7.620   1.00 49.91  ? 504 NAG   A O5  1 
HETATM 2714 O  O6  . NAG   E 2 .   ? -12.245 19.415  8.679   1.00 56.56  ? 504 NAG   A O6  1 
HETATM 2715 O  O7  . NAG   E 2 .   ? -14.573 13.176  9.083   1.00 58.24  ? 504 NAG   A O7  1 
HETATM 2716 C  C1  . NAG   F 2 .   ? -32.243 18.282  -12.685 1.00 46.84  ? 505 NAG   A C1  1 
HETATM 2717 C  C2  . NAG   F 2 .   ? -33.714 18.279  -13.096 1.00 49.28  ? 505 NAG   A C2  1 
HETATM 2718 C  C3  . NAG   F 2 .   ? -34.398 19.559  -12.625 1.00 48.82  ? 505 NAG   A C3  1 
HETATM 2719 C  C4  . NAG   F 2 .   ? -34.177 19.769  -11.133 1.00 46.40  ? 505 NAG   A C4  1 
HETATM 2720 C  C5  . NAG   F 2 .   ? -32.690 19.699  -10.799 1.00 48.42  ? 505 NAG   A C5  1 
HETATM 2721 C  C6  . NAG   F 2 .   ? -32.420 19.730  -9.314  1.00 47.55  ? 505 NAG   A C6  1 
HETATM 2722 C  C7  . NAG   F 2 .   ? -34.189 16.973  -15.120 1.00 49.78  ? 505 NAG   A C7  1 
HETATM 2723 C  C8  . NAG   F 2 .   ? -34.280 16.995  -16.616 1.00 52.59  ? 505 NAG   A C8  1 
HETATM 2724 N  N2  . NAG   F 2 .   ? -33.850 18.127  -14.536 1.00 46.24  ? 505 NAG   A N2  1 
HETATM 2725 O  O3  . NAG   F 2 .   ? -35.793 19.472  -12.893 1.00 57.35  ? 505 NAG   A O3  1 
HETATM 2726 O  O4  . NAG   F 2 .   ? -34.675 21.044  -10.747 1.00 45.34  ? 505 NAG   A O4  1 
HETATM 2727 O  O5  . NAG   F 2 .   ? -32.140 18.466  -11.281 1.00 48.09  ? 505 NAG   A O5  1 
HETATM 2728 O  O6  . NAG   F 2 .   ? -31.033 19.583  -9.044  1.00 48.70  ? 505 NAG   A O6  1 
HETATM 2729 O  O7  . NAG   F 2 .   ? -34.414 15.958  -14.469 1.00 53.80  ? 505 NAG   A O7  1 
HETATM 2730 C  C1  . NAG   G 2 .   ? -19.206 22.845  -34.065 1.00 50.97  ? 506 NAG   A C1  1 
HETATM 2731 C  C2  . NAG   G 2 .   ? -20.482 22.669  -34.888 1.00 50.68  ? 506 NAG   A C2  1 
HETATM 2732 C  C3  . NAG   G 2 .   ? -20.181 22.835  -36.374 1.00 52.96  ? 506 NAG   A C3  1 
HETATM 2733 C  C4  . NAG   G 2 .   ? -19.490 24.167  -36.626 1.00 60.23  ? 506 NAG   A C4  1 
HETATM 2734 C  C5  . NAG   G 2 .   ? -18.238 24.270  -35.763 1.00 56.93  ? 506 NAG   A C5  1 
HETATM 2735 C  C6  . NAG   G 2 .   ? -17.558 25.614  -35.872 1.00 51.72  ? 506 NAG   A C6  1 
HETATM 2736 C  C7  . NAG   G 2 .   ? -22.073 21.191  -33.740 1.00 52.23  ? 506 NAG   A C7  1 
HETATM 2737 C  C8  . NAG   G 2 .   ? -22.584 19.788  -33.605 1.00 48.57  ? 506 NAG   A C8  1 
HETATM 2738 N  N2  . NAG   G 2 .   ? -21.093 21.374  -34.631 1.00 50.96  ? 506 NAG   A N2  1 
HETATM 2739 O  O3  . NAG   G 2 .   ? -21.396 22.771  -37.112 1.00 54.69  ? 506 NAG   A O3  1 
HETATM 2740 O  O4  . NAG   G 2 .   ? -19.134 24.286  -37.999 1.00 68.25  ? 506 NAG   A O4  1 
HETATM 2741 O  O5  . NAG   G 2 .   ? -18.593 24.102  -34.383 1.00 51.94  ? 506 NAG   A O5  1 
HETATM 2742 O  O6  . NAG   G 2 .   ? -18.347 26.642  -35.288 1.00 57.18  ? 506 NAG   A O6  1 
HETATM 2743 O  O7  . NAG   G 2 .   ? -22.525 22.115  -33.071 1.00 54.45  ? 506 NAG   A O7  1 
HETATM 2744 C  C1  . NAG   H 2 .   ? -29.597 27.233  -26.707 1.00 49.80  ? 507 NAG   A C1  1 
HETATM 2745 C  C2  . NAG   H 2 .   ? -30.172 27.023  -28.113 1.00 51.74  ? 507 NAG   A C2  1 
HETATM 2746 C  C3  . NAG   H 2 .   ? -31.682 27.261  -28.133 1.00 53.67  ? 507 NAG   A C3  1 
HETATM 2747 C  C4  . NAG   H 2 .   ? -32.373 26.484  -27.021 1.00 56.08  ? 507 NAG   A C4  1 
HETATM 2748 C  C5  . NAG   H 2 .   ? -31.713 26.801  -25.687 1.00 57.55  ? 507 NAG   A C5  1 
HETATM 2749 C  C6  . NAG   H 2 .   ? -32.284 26.007  -24.537 1.00 51.01  ? 507 NAG   A C6  1 
HETATM 2750 C  C7  . NAG   H 2 .   ? -28.891 27.449  -30.168 1.00 54.04  ? 507 NAG   A C7  1 
HETATM 2751 C  C8  . NAG   H 2 .   ? -28.262 28.496  -31.039 1.00 56.00  ? 507 NAG   A C8  1 
HETATM 2752 N  N2  . NAG   H 2 .   ? -29.509 27.896  -29.070 1.00 54.78  ? 507 NAG   A N2  1 
HETATM 2753 O  O3  . NAG   H 2 .   ? -32.191 26.834  -29.391 1.00 56.04  ? 507 NAG   A O3  1 
HETATM 2754 O  O4  . NAG   H 2 .   ? -33.751 26.831  -26.962 1.00 59.27  ? 507 NAG   A O4  1 
HETATM 2755 O  O5  . NAG   H 2 .   ? -30.325 26.464  -25.769 1.00 54.16  ? 507 NAG   A O5  1 
HETATM 2756 O  O6  . NAG   H 2 .   ? -31.818 24.665  -24.556 1.00 53.99  ? 507 NAG   A O6  1 
HETATM 2757 O  O7  . NAG   H 2 .   ? -28.843 26.256  -30.448 1.00 55.14  ? 507 NAG   A O7  1 
HETATM 2758 C  C1  . NAG   I 2 .   ? -8.996  33.592  -18.891 1.00 39.94  ? 508 NAG   A C1  1 
HETATM 2759 C  C2  . NAG   I 2 .   ? -7.615  33.850  -18.272 1.00 44.10  ? 508 NAG   A C2  1 
HETATM 2760 C  C3  . NAG   I 2 .   ? -7.673  35.013  -17.280 1.00 48.22  ? 508 NAG   A C3  1 
HETATM 2761 C  C4  . NAG   I 2 .   ? -8.362  36.227  -17.888 1.00 45.90  ? 508 NAG   A C4  1 
HETATM 2762 C  C5  . NAG   I 2 .   ? -9.715  35.817  -18.449 1.00 46.24  ? 508 NAG   A C5  1 
HETATM 2763 C  C6  . NAG   I 2 .   ? -10.452 36.948  -19.127 1.00 46.00  ? 508 NAG   A C6  1 
HETATM 2764 C  C7  . NAG   I 2 .   ? -5.851  32.275  -17.591 1.00 51.19  ? 508 NAG   A C7  1 
HETATM 2765 C  C8  . NAG   I 2 .   ? -5.549  31.007  -16.850 1.00 46.49  ? 508 NAG   A C8  1 
HETATM 2766 N  N2  . NAG   I 2 .   ? -7.133  32.650  -17.607 1.00 45.32  ? 508 NAG   A N2  1 
HETATM 2767 O  O3  . NAG   I 2 .   ? -6.349  35.354  -16.884 1.00 49.10  ? 508 NAG   A O3  1 
HETATM 2768 O  O4  . NAG   I 2 .   ? -8.549  37.227  -16.893 1.00 46.79  ? 508 NAG   A O4  1 
HETATM 2769 O  O5  . NAG   I 2 .   ? -9.514  34.799  -19.435 1.00 47.16  ? 508 NAG   A O5  1 
HETATM 2770 O  O6  . NAG   I 2 .   ? -9.937  37.194  -20.428 1.00 53.24  ? 508 NAG   A O6  1 
HETATM 2771 O  O7  . NAG   I 2 .   ? -4.975  32.927  -18.151 1.00 55.31  ? 508 NAG   A O7  1 
HETATM 2772 C  C1  . NAG   J 2 .   ? -24.700 13.303  -25.330 1.00 58.11  ? 509 NAG   A C1  1 
HETATM 2773 C  C2  . NAG   J 2 .   ? -24.476 11.795  -25.518 1.00 60.73  ? 509 NAG   A C2  1 
HETATM 2774 C  C3  . NAG   J 2 .   ? -25.695 11.128  -26.157 1.00 65.87  ? 509 NAG   A C3  1 
HETATM 2775 C  C4  . NAG   J 2 .   ? -26.975 11.509  -25.429 1.00 67.68  ? 509 NAG   A C4  1 
HETATM 2776 C  C5  . NAG   J 2 .   ? -27.083 13.023  -25.354 1.00 65.11  ? 509 NAG   A C5  1 
HETATM 2777 C  C6  . NAG   J 2 .   ? -28.296 13.499  -24.590 1.00 65.39  ? 509 NAG   A C6  1 
HETATM 2778 C  C7  . NAG   J 2 .   ? -22.226 10.870  -25.894 1.00 58.84  ? 509 NAG   A C7  1 
HETATM 2779 C  C8  . NAG   J 2 .   ? -21.099 10.727  -26.870 1.00 51.80  ? 509 NAG   A C8  1 
HETATM 2780 N  N2  . NAG   J 2 .   ? -23.289 11.556  -26.325 1.00 60.85  ? 509 NAG   A N2  1 
HETATM 2781 O  O3  . NAG   J 2 .   ? -25.520 9.716   -26.106 1.00 66.82  ? 509 NAG   A O3  1 
HETATM 2782 O  O4  . NAG   J 2 .   ? -28.105 10.989  -26.119 1.00 74.38  ? 509 NAG   A O4  1 
HETATM 2783 O  O5  . NAG   J 2 .   ? -25.936 13.530  -24.663 1.00 62.62  ? 509 NAG   A O5  1 
HETATM 2784 O  O6  . NAG   J 2 .   ? -27.920 14.220  -23.424 1.00 59.65  ? 509 NAG   A O6  1 
HETATM 2785 O  O7  . NAG   J 2 .   ? -22.176 10.385  -24.767 1.00 56.09  ? 509 NAG   A O7  1 
HETATM 2786 N  N1  . EPE   K 3 .   ? -5.191  -5.874  -17.083 1.00 38.87  ? 510 EPE   A N1  1 
HETATM 2787 C  C2  . EPE   K 3 .   ? -4.671  -5.277  -15.848 1.00 36.07  ? 510 EPE   A C2  1 
HETATM 2788 C  C3  . EPE   K 3 .   ? -5.824  -5.115  -14.863 1.00 38.39  ? 510 EPE   A C3  1 
HETATM 2789 N  N4  . EPE   K 3 .   ? -7.038  -4.573  -15.455 1.00 38.27  ? 510 EPE   A N4  1 
HETATM 2790 C  C5  . EPE   K 3 .   ? -7.339  -4.864  -16.839 1.00 37.30  ? 510 EPE   A C5  1 
HETATM 2791 C  C6  . EPE   K 3 .   ? -6.100  -4.918  -17.715 1.00 36.88  ? 510 EPE   A C6  1 
HETATM 2792 C  C7  . EPE   K 3 .   ? -8.177  -4.290  -14.601 1.00 35.46  ? 510 EPE   A C7  1 
HETATM 2793 C  C8  . EPE   K 3 .   ? -7.915  -3.198  -13.570 1.00 37.62  ? 510 EPE   A C8  1 
HETATM 2794 O  O8  . EPE   K 3 .   ? -7.114  -3.686  -12.517 1.00 41.87  ? 510 EPE   A O8  1 
HETATM 2795 C  C9  . EPE   K 3 .   ? -4.096  -6.156  -18.008 1.00 37.77  ? 510 EPE   A C9  1 
HETATM 2796 C  C10 . EPE   K 3 .   ? -4.374  -7.484  -18.695 1.00 30.10  ? 510 EPE   A C10 1 
HETATM 2797 S  S   . EPE   K 3 .   ? -2.903  -7.967  -19.618 1.00 34.00  ? 510 EPE   A S   1 
HETATM 2798 O  O1S . EPE   K 3 .   ? -2.426  -6.810  -20.368 1.00 36.32  ? 510 EPE   A O1S 1 
HETATM 2799 O  O2S . EPE   K 3 .   ? -1.894  -8.377  -18.649 1.00 31.74  ? 510 EPE   A O2S 1 
HETATM 2800 O  O3S . EPE   K 3 .   ? -3.216  -9.061  -20.530 1.00 34.03  ? 510 EPE   A O3S 1 
HETATM 2801 O  O   . A1ATK L 4 .   ? 1.011   11.340  -7.970  1.00 65.07  ? 511 A1ATK A O   1 
HETATM 2802 C  C10 . A1ATK L 4 .   ? -3.137  17.450  -14.783 1.00 34.33  ? 511 A1ATK A C10 1 
HETATM 2803 N  N   . A1ATK L 4 .   ? -0.518  9.359   -7.642  1.00 65.20  ? 511 A1ATK A N   1 
HETATM 2804 C  CA  . A1ATK L 4 .   ? -1.226  10.622  -7.666  1.00 65.83  ? 511 A1ATK A CA  1 
HETATM 2805 C  CB  . A1ATK L 4 .   ? -1.728  10.762  -6.225  1.00 67.73  ? 511 A1ATK A CB  1 
HETATM 2806 C  CG  . A1ATK L 4 .   ? -2.267  9.367   -5.752  1.00 61.44  ? 511 A1ATK A CG  1 
HETATM 2807 C  CD  . A1ATK L 4 .   ? -2.242  9.063   -4.217  1.00 61.60  ? 511 A1ATK A CD  1 
HETATM 2808 N  NE  . A1ATK L 4 .   ? -1.863  7.683   -3.833  1.00 67.21  ? 511 A1ATK A NE  1 
HETATM 2809 C  CZ  . A1ATK L 4 .   ? -2.719  6.800   -2.965  1.00 68.00  ? 511 A1ATK A CZ  1 
HETATM 2810 N  NH1 . A1ATK L 4 .   ? -2.348  5.615   -2.635  1.00 69.20  ? 511 A1ATK A NH1 1 
HETATM 2811 N  NH2 . A1ATK L 4 .   ? -3.845  7.254   -2.555  1.00 66.87  ? 511 A1ATK A NH2 1 
HETATM 2812 C  C01 . A1ATK L 4 .   ? -0.130  11.584  -8.258  1.00 61.54  ? 511 A1ATK A C01 1 
HETATM 2813 C  C03 . A1ATK L 4 .   ? -1.495  13.317  -9.808  1.00 51.84  ? 511 A1ATK A C03 1 
HETATM 2814 C  C04 . A1ATK L 4 .   ? -1.305  14.553  -10.743 1.00 48.51  ? 511 A1ATK A C04 1 
HETATM 2815 C  C06 . A1ATK L 4 .   ? -0.123  17.003  -10.720 1.00 52.40  ? 511 A1ATK A C06 1 
HETATM 2816 C  C08 . A1ATK L 4 .   ? -2.303  17.522  -12.285 1.00 36.19  ? 511 A1ATK A C08 1 
HETATM 2817 C  C09 . A1ATK L 4 .   ? -1.959  17.711  -13.791 1.00 33.89  ? 511 A1ATK A C09 1 
HETATM 2818 C  C13 . A1ATK L 4 .   ? -3.530  17.016  -17.347 1.00 24.96  ? 511 A1ATK A C13 1 
HETATM 2819 C  C14 . A1ATK L 4 .   ? -4.898  17.056  -17.292 1.00 24.79  ? 511 A1ATK A C14 1 
HETATM 2820 C  C15 . A1ATK L 4 .   ? -5.624  16.828  -18.430 1.00 25.31  ? 511 A1ATK A C15 1 
HETATM 2821 C  C17 . A1ATK L 4 .   ? -4.975  16.568  -19.624 1.00 27.44  ? 511 A1ATK A C17 1 
HETATM 2822 C  C19 . A1ATK L 4 .   ? -3.608  16.536  -19.686 1.00 27.75  ? 511 A1ATK A C19 1 
HETATM 2823 C  C20 . A1ATK L 4 .   ? -2.886  16.761  -18.551 1.00 27.18  ? 511 A1ATK A C20 1 
HETATM 2824 C  C21 . A1ATK L 4 .   ? -1.520  19.088  -14.105 1.00 30.69  ? 511 A1ATK A C21 1 
HETATM 2825 C  C22 . A1ATK L 4 .   ? -0.415  19.584  -13.262 1.00 36.75  ? 511 A1ATK A C22 1 
HETATM 2826 C  C23 . A1ATK L 4 .   ? -0.708  19.312  -11.769 1.00 41.44  ? 511 A1ATK A C23 1 
HETATM 2827 C  C25 . A1ATK L 4 .   ? 0.771   14.950  -9.529  1.00 58.82  ? 511 A1ATK A C25 1 
HETATM 2828 C  C26 . A1ATK L 4 .   ? 0.898   13.443  -9.660  1.00 54.06  ? 511 A1ATK A C26 1 
HETATM 2829 F  F16 . A1ATK L 4 .   ? -6.978  16.856  -18.380 1.00 28.46  ? 511 A1ATK A F16 1 
HETATM 2830 N  N02 . A1ATK L 4 .   ? -0.293  12.731  -9.205  1.00 57.23  ? 511 A1ATK A N02 1 
HETATM 2831 N  N05 . A1ATK L 4 .   ? -0.261  15.526  -10.376 1.00 57.62  ? 511 A1ATK A N05 1 
HETATM 2832 N  N07 . A1ATK L 4 .   ? -1.039  17.873  -11.546 1.00 38.66  ? 511 A1ATK A N07 1 
HETATM 2833 N  N12 . A1ATK L 4 .   ? -2.698  17.257  -16.200 1.00 27.16  ? 511 A1ATK A N12 1 
HETATM 2834 O  O11 . A1ATK L 4 .   ? -4.261  17.429  -14.444 1.00 32.94  ? 511 A1ATK A O11 1 
HETATM 2835 O  O24 . A1ATK L 4 .   ? 0.830   17.552  -10.270 1.00 60.08  ? 511 A1ATK A O24 1 
HETATM 2836 CL CL1 . A1ATK L 4 .   ? -5.909  16.260  -21.103 1.00 36.44  ? 511 A1ATK A CL1 1 
HETATM 2837 C  C1  . MPD   M 5 .   ? -16.508 23.804  10.452  1.00 62.91  ? 512 MPD   A C1  1 
HETATM 2838 C  C2  . MPD   M 5 .   ? -15.058 23.942  10.001  1.00 73.63  ? 512 MPD   A C2  1 
HETATM 2839 O  O2  . MPD   M 5 .   ? -15.014 24.191  8.568   1.00 77.48  ? 512 MPD   A O2  1 
HETATM 2840 C  CM  . MPD   M 5 .   ? -14.361 22.625  10.274  1.00 67.45  ? 512 MPD   A CM  1 
HETATM 2841 C  C3  . MPD   M 5 .   ? -14.362 25.084  10.737  1.00 63.55  ? 512 MPD   A C3  1 
HETATM 2842 C  C4  . MPD   M 5 .   ? -13.043 25.489  10.080  1.00 74.02  ? 512 MPD   A C4  1 
HETATM 2843 O  O4  . MPD   M 5 .   ? -13.023 26.884  9.932   1.00 64.95  ? 512 MPD   A O4  1 
HETATM 2844 C  C5  . MPD   M 5 .   ? -11.817 25.066  10.888  1.00 60.47  ? 512 MPD   A C5  1 
HETATM 2845 O  O   . HOH   N 6 .   ? -23.038 -8.549  -14.511 1.00 53.79  ? 601 HOH   A O   1 
HETATM 2846 O  O   . HOH   N 6 .   ? -14.351 0.025   -30.577 1.00 46.68  ? 602 HOH   A O   1 
HETATM 2847 O  O   . HOH   N 6 .   ? -0.607  31.460  -37.672 1.00 46.29  ? 603 HOH   A O   1 
HETATM 2848 O  O   . HOH   N 6 .   ? -5.069  32.516  -8.869  1.00 59.16  ? 604 HOH   A O   1 
HETATM 2849 O  O   . HOH   N 6 .   ? -22.875 21.027  -37.185 1.00 57.50  ? 605 HOH   A O   1 
HETATM 2850 O  O   . HOH   N 6 .   ? -26.376 19.906  -25.779 1.00 53.08  ? 606 HOH   A O   1 
HETATM 2851 O  O   . HOH   N 6 .   ? -18.236 1.837   -2.390  1.00 38.37  ? 607 HOH   A O   1 
HETATM 2852 O  O   . HOH   N 6 .   ? -12.358 -3.470  -4.293  1.00 42.69  ? 608 HOH   A O   1 
HETATM 2853 O  O   . HOH   N 6 .   ? -26.971 -4.098  -14.366 1.00 49.20  ? 609 HOH   A O   1 
HETATM 2854 O  O   . HOH   N 6 .   ? -16.995 14.895  -31.967 1.00 36.49  ? 610 HOH   A O   1 
HETATM 2855 O  O   . HOH   N 6 .   ? -18.240 11.268  -15.914 1.00 33.67  ? 611 HOH   A O   1 
HETATM 2856 O  O   . HOH   N 6 .   ? -19.432 33.403  -28.813 1.00 42.00  ? 612 HOH   A O   1 
HETATM 2857 O  O   . HOH   N 6 .   ? -26.435 9.006   -8.173  1.00 37.03  ? 613 HOH   A O   1 
HETATM 2858 O  O   . HOH   N 6 .   ? -24.069 37.333  -0.050  1.00 53.67  ? 614 HOH   A O   1 
HETATM 2859 O  O   . HOH   N 6 .   ? -6.595  35.254  -14.509 1.00 51.96  ? 615 HOH   A O   1 
HETATM 2860 O  O   . HOH   N 6 .   ? -32.256 -10.767 0.314   1.00 57.67  ? 616 HOH   A O   1 
HETATM 2861 O  O   . HOH   N 6 .   ? -13.966 14.029  -18.333 1.00 28.57  ? 617 HOH   A O   1 
HETATM 2862 O  O   . HOH   N 6 .   ? -17.048 34.150  1.766   1.00 49.78  ? 618 HOH   A O   1 
HETATM 2863 O  O   . HOH   N 6 .   ? 0.970   28.791  -31.409 1.00 41.96  ? 619 HOH   A O   1 
HETATM 2864 O  O   . HOH   N 6 .   ? -18.658 3.088   -5.274  1.00 35.03  ? 620 HOH   A O   1 
HETATM 2865 O  O   . HOH   N 6 .   ? -22.999 32.775  -19.113 1.00 48.91  ? 621 HOH   A O   1 
HETATM 2866 O  O   . HOH   N 6 .   ? -28.652 8.919   -10.242 1.00 44.78  ? 622 HOH   A O   1 
HETATM 2867 O  O   . HOH   N 6 .   ? -15.998 18.716  -0.025  1.00 38.55  ? 623 HOH   A O   1 
HETATM 2868 O  O   . HOH   N 6 .   ? -15.298 18.870  -26.404 1.00 32.10  ? 624 HOH   A O   1 
HETATM 2869 O  O   . HOH   N 6 .   ? -3.783  12.064  -35.097 1.00 37.96  ? 625 HOH   A O   1 
HETATM 2870 O  O   . HOH   N 6 .   ? -10.316 7.522   -34.172 1.00 40.38  ? 626 HOH   A O   1 
HETATM 2871 O  O   . HOH   N 6 .   ? -10.026 14.933  -5.083  1.00 39.01  ? 627 HOH   A O   1 
HETATM 2872 O  O   . HOH   N 6 .   ? -12.797 11.641  -28.643 1.00 37.79  ? 628 HOH   A O   1 
HETATM 2873 O  O   . HOH   N 6 .   ? -31.620 12.889  -7.804  1.00 48.31  ? 629 HOH   A O   1 
HETATM 2874 O  O   . HOH   N 6 .   ? -4.695  22.298  -41.054 1.00 44.99  ? 630 HOH   A O   1 
HETATM 2875 O  O   . HOH   N 6 .   ? -21.312 2.875   -21.911 1.00 48.68  ? 631 HOH   A O   1 
HETATM 2876 O  O   . HOH   N 6 .   ? -29.825 20.477  -15.557 1.00 41.55  ? 632 HOH   A O   1 
HETATM 2877 O  O   . HOH   N 6 .   ? 0.687   12.309  -21.446 1.00 41.49  ? 633 HOH   A O   1 
HETATM 2878 O  O   . HOH   N 6 .   ? -20.455 38.017  3.825   1.00 44.87  ? 634 HOH   A O   1 
HETATM 2879 O  O   . HOH   N 6 .   ? -3.080  1.423   -27.684 1.00 31.02  ? 635 HOH   A O   1 
HETATM 2880 O  O   . HOH   N 6 .   ? -15.928 1.481   -1.314  1.00 41.87  ? 636 HOH   A O   1 
HETATM 2881 O  O   . HOH   N 6 .   ? -10.836 12.353  -24.934 1.00 27.71  ? 637 HOH   A O   1 
HETATM 2882 O  O   . HOH   N 6 .   ? -8.296  27.511  -7.432  1.00 40.15  ? 638 HOH   A O   1 
HETATM 2883 O  O   . HOH   N 6 .   ? -2.715  31.778  -17.899 1.00 49.43  ? 639 HOH   A O   1 
HETATM 2884 O  O   . HOH   N 6 .   ? -16.486 29.256  0.247   1.00 38.16  ? 640 HOH   A O   1 
HETATM 2885 O  O   . HOH   N 6 .   ? -11.086 10.364  -33.531 1.00 44.75  ? 641 HOH   A O   1 
HETATM 2886 O  O   . HOH   N 6 .   ? -20.896 25.151  -32.185 1.00 48.64  ? 642 HOH   A O   1 
HETATM 2887 O  O   . HOH   N 6 .   ? -16.828 8.268   -18.656 1.00 27.69  ? 643 HOH   A O   1 
HETATM 2888 O  O   . HOH   N 6 .   ? -16.252 -1.237  -25.313 1.00 42.80  ? 644 HOH   A O   1 
HETATM 2889 O  O   . HOH   N 6 .   ? -16.538 11.155  -18.239 1.00 23.31  ? 645 HOH   A O   1 
HETATM 2890 O  O   . HOH   N 6 .   ? -31.417 -4.226  -2.581  1.00 53.41  ? 646 HOH   A O   1 
HETATM 2891 O  O   . HOH   N 6 .   ? -0.698  15.595  -28.765 1.00 32.01  ? 647 HOH   A O   1 
HETATM 2892 O  O   . HOH   N 6 .   ? -9.218  11.336  -5.665  1.00 36.66  ? 648 HOH   A O   1 
HETATM 2893 O  O   . HOH   N 6 .   ? -7.766  31.067  -13.054 1.00 43.94  ? 649 HOH   A O   1 
HETATM 2894 O  O   . HOH   N 6 .   ? -16.198 24.783  -32.533 1.00 40.01  ? 650 HOH   A O   1 
HETATM 2895 O  O   . HOH   N 6 .   ? -30.078 11.928  -9.797  1.00 43.48  ? 651 HOH   A O   1 
HETATM 2896 O  O   . HOH   N 6 .   ? -11.627 26.868  -4.035  1.00 37.34  ? 652 HOH   A O   1 
HETATM 2897 O  O   . HOH   N 6 .   ? -10.172 14.343  -23.047 1.00 26.31  ? 653 HOH   A O   1 
HETATM 2898 O  O   . HOH   N 6 .   ? -9.433  16.287  -13.403 1.00 24.50  ? 654 HOH   A O   1 
HETATM 2899 O  O   . HOH   N 6 .   ? -13.923 38.273  -9.809  1.00 48.99  ? 655 HOH   A O   1 
HETATM 2900 O  O   . HOH   N 6 .   ? -10.103 9.283   -1.929  1.00 61.38  ? 656 HOH   A O   1 
HETATM 2901 O  O   . HOH   N 6 .   ? 0.320   19.721  -30.263 1.00 34.49  ? 657 HOH   A O   1 
HETATM 2902 O  O   . HOH   N 6 .   ? -7.091  32.500  -21.761 1.00 38.84  ? 658 HOH   A O   1 
HETATM 2903 O  O   . HOH   N 6 .   ? -30.839 22.209  -9.140  1.00 49.27  ? 659 HOH   A O   1 
HETATM 2904 O  O   . HOH   N 6 .   ? -1.847  -0.855  -26.283 1.00 38.01  ? 660 HOH   A O   1 
HETATM 2905 O  O   . HOH   N 6 .   ? -8.316  8.248   -22.336 1.00 24.18  ? 661 HOH   A O   1 
HETATM 2906 O  O   . HOH   N 6 .   ? -10.721 12.283  -29.598 1.00 35.94  ? 662 HOH   A O   1 
HETATM 2907 O  O   . HOH   N 6 .   ? -5.044  11.414  -2.772  1.00 54.42  ? 663 HOH   A O   1 
HETATM 2908 O  O   . HOH   N 6 .   ? -29.310 16.095  -5.021  1.00 44.10  ? 664 HOH   A O   1 
HETATM 2909 O  O   . HOH   N 6 .   ? -21.708 5.468   -13.956 1.00 36.74  ? 665 HOH   A O   1 
HETATM 2910 O  O   . HOH   N 6 .   ? -10.332 24.826  -8.015  1.00 36.21  ? 666 HOH   A O   1 
HETATM 2911 O  O   . HOH   N 6 .   ? -9.850  29.156  -17.365 1.00 34.53  ? 667 HOH   A O   1 
HETATM 2912 O  O   . HOH   N 6 .   ? -22.069 11.803  -22.515 1.00 41.29  ? 668 HOH   A O   1 
HETATM 2913 O  O   . HOH   N 6 .   ? 0.898   25.344  -16.184 1.00 33.17  ? 669 HOH   A O   1 
HETATM 2914 O  O   . HOH   N 6 .   ? -23.902 23.980  -25.696 1.00 36.67  ? 670 HOH   A O   1 
HETATM 2915 O  O   . HOH   N 6 .   ? -13.768 32.042  -21.011 1.00 31.73  ? 671 HOH   A O   1 
HETATM 2916 O  O   . HOH   N 6 .   ? -17.632 28.010  5.170   1.00 49.23  ? 672 HOH   A O   1 
HETATM 2917 O  O   . HOH   N 6 .   ? -20.674 5.812   -17.927 1.00 34.63  ? 673 HOH   A O   1 
HETATM 2918 O  O   . HOH   N 6 .   ? -18.360 34.197  -26.104 1.00 40.73  ? 674 HOH   A O   1 
HETATM 2919 O  O   . HOH   N 6 .   ? -14.241 21.873  -1.724  1.00 38.06  ? 675 HOH   A O   1 
HETATM 2920 O  O   . HOH   N 6 .   ? -20.244 11.440  -2.201  1.00 35.47  ? 676 HOH   A O   1 
HETATM 2921 O  O   . HOH   N 6 .   ? -15.392 8.826   -27.205 1.00 33.23  ? 677 HOH   A O   1 
HETATM 2922 O  O   . HOH   N 6 .   ? -17.994 -12.052 -11.270 1.00 44.01  ? 678 HOH   A O   1 
HETATM 2923 O  O   . HOH   N 6 .   ? -14.856 -2.070  -4.357  1.00 38.02  ? 679 HOH   A O   1 
HETATM 2924 O  O   . HOH   N 6 .   ? -18.655 -7.377  -20.289 1.00 45.48  ? 680 HOH   A O   1 
HETATM 2925 O  O   . HOH   N 6 .   ? -25.589 14.656  -2.430  1.00 42.28  ? 681 HOH   A O   1 
HETATM 2926 O  O   . HOH   N 6 .   ? -8.397  -7.746  -18.484 1.00 29.66  ? 682 HOH   A O   1 
HETATM 2927 O  O   . HOH   N 6 .   ? -20.709 11.434  -10.924 1.00 35.41  ? 683 HOH   A O   1 
HETATM 2928 O  O   . HOH   N 6 .   ? -18.989 19.269  -35.099 1.00 44.26  ? 684 HOH   A O   1 
HETATM 2929 O  O   . HOH   N 6 .   ? -4.277  11.968  -12.103 1.00 36.69  ? 685 HOH   A O   1 
HETATM 2930 O  O   . HOH   N 6 .   ? -10.809 4.996   -4.096  1.00 42.23  ? 686 HOH   A O   1 
HETATM 2931 O  O   . HOH   N 6 .   ? -4.346  -5.051  -29.836 1.00 37.20  ? 687 HOH   A O   1 
HETATM 2932 O  O   . HOH   N 6 .   ? -16.334 15.781  -34.647 1.00 40.99  ? 688 HOH   A O   1 
HETATM 2933 O  O   . HOH   N 6 .   ? -14.889 10.330  -25.044 1.00 27.66  ? 689 HOH   A O   1 
HETATM 2934 O  O   . HOH   N 6 .   ? -16.891 -11.115 -14.125 1.00 43.12  ? 690 HOH   A O   1 
HETATM 2935 O  O   . HOH   N 6 .   ? -1.595  21.961  -37.422 1.00 37.53  ? 691 HOH   A O   1 
HETATM 2936 O  O   . HOH   N 6 .   ? 2.527   16.221  -13.524 1.00 43.89  ? 692 HOH   A O   1 
HETATM 2937 O  O   . HOH   N 6 .   ? -10.221 24.644  -0.578  1.00 45.23  ? 693 HOH   A O   1 
HETATM 2938 O  O   . HOH   N 6 .   ? -8.015  17.255  -38.919 1.00 42.83  ? 694 HOH   A O   1 
HETATM 2939 O  O   . HOH   N 6 .   ? -34.212 3.302   -3.283  1.00 52.54  ? 695 HOH   A O   1 
HETATM 2940 O  O   . HOH   N 6 .   ? -1.233  18.421  -28.091 1.00 24.92  ? 696 HOH   A O   1 
HETATM 2941 O  O   . HOH   N 6 .   ? -16.788 21.803  -0.216  1.00 37.79  ? 697 HOH   A O   1 
HETATM 2942 O  O   . HOH   N 6 .   ? 0.363   4.513   -29.824 1.00 44.65  ? 698 HOH   A O   1 
HETATM 2943 O  O   . HOH   N 6 .   ? -0.947  13.578  -19.441 1.00 33.12  ? 699 HOH   A O   1 
HETATM 2944 O  O   . HOH   N 6 .   ? -12.974 14.724  5.950   1.00 46.56  ? 700 HOH   A O   1 
HETATM 2945 O  O   . HOH   N 6 .   ? -13.992 20.033  -24.054 1.00 33.39  ? 701 HOH   A O   1 
HETATM 2946 O  O   . HOH   N 6 .   ? -7.593  10.663  -33.518 1.00 37.47  ? 702 HOH   A O   1 
HETATM 2947 O  O   . HOH   N 6 .   ? -14.241 14.576  -1.836  1.00 36.40  ? 703 HOH   A O   1 
HETATM 2948 O  O   . HOH   N 6 .   ? -31.107 12.494  -16.592 1.00 39.80  ? 704 HOH   A O   1 
HETATM 2949 O  O   . HOH   N 6 .   ? -14.193 10.536  -17.494 1.00 33.61  ? 705 HOH   A O   1 
HETATM 2950 O  O   . HOH   N 6 .   ? -3.237  13.979  -32.890 1.00 35.62  ? 706 HOH   A O   1 
HETATM 2951 O  O   . HOH   N 6 .   ? -3.343  5.209   -33.691 1.00 38.31  ? 707 HOH   A O   1 
HETATM 2952 O  O   . HOH   N 6 .   ? -7.559  -2.743  -32.072 1.00 54.88  ? 708 HOH   A O   1 
HETATM 2953 O  O   . HOH   N 6 .   ? -1.225  -4.303  -20.865 1.00 37.74  ? 709 HOH   A O   1 
HETATM 2954 O  O   . HOH   N 6 .   ? -19.340 -1.614  -24.248 1.00 46.51  ? 710 HOH   A O   1 
HETATM 2955 O  O   . HOH   N 6 .   ? -0.164  1.803   -15.008 1.00 32.93  ? 711 HOH   A O   1 
HETATM 2956 O  O   . HOH   N 6 .   ? -20.638 12.589  -15.494 1.00 35.21  ? 712 HOH   A O   1 
HETATM 2957 O  O   . HOH   N 6 .   ? -26.915 16.553  -4.131  1.00 40.12  ? 713 HOH   A O   1 
HETATM 2958 O  O   . HOH   N 6 .   ? -27.717 19.177  -15.561 1.00 44.96  ? 714 HOH   A O   1 
HETATM 2959 O  O   . HOH   N 6 .   ? -18.537 6.774   -19.801 1.00 31.72  ? 715 HOH   A O   1 
HETATM 2960 O  O   . HOH   N 6 .   ? -12.490 29.455  -14.783 1.00 37.99  ? 716 HOH   A O   1 
HETATM 2961 O  O   . HOH   N 6 .   ? -35.456 26.596  -29.242 1.00 40.81  ? 717 HOH   A O   1 
HETATM 2962 O  O   . HOH   N 6 .   ? -1.812  12.094  -31.853 1.00 36.78  ? 718 HOH   A O   1 
HETATM 2963 O  O   . HOH   N 6 .   ? -11.899 -0.771  -1.785  1.00 38.98  ? 719 HOH   A O   1 
HETATM 2964 O  O   . HOH   N 6 .   ? -6.518  -8.297  -16.306 1.00 37.20  ? 720 HOH   A O   1 
HETATM 2965 O  O   . HOH   N 6 .   ? -28.808 39.351  -18.307 1.00 56.08  ? 721 HOH   A O   1 
HETATM 2966 O  O   . HOH   N 6 .   ? -12.280 27.578  6.918   1.00 55.89  ? 722 HOH   A O   1 
HETATM 2967 O  O   . HOH   N 6 .   ? -26.344 7.371   0.951   1.00 45.84  ? 723 HOH   A O   1 
HETATM 2968 O  O   . HOH   N 6 .   ? -15.120 28.313  3.835   1.00 51.20  ? 724 HOH   A O   1 
HETATM 2969 O  O   . HOH   N 6 .   ? -7.005  30.340  -24.226 1.00 40.01  ? 725 HOH   A O   1 
HETATM 2970 O  O   . HOH   N 6 .   ? 11.821  13.502  -29.518 1.00 53.56  ? 726 HOH   A O   1 
HETATM 2971 O  O   . HOH   N 6 .   ? -25.833 28.947  -28.547 1.00 42.07  ? 727 HOH   A O   1 
HETATM 2972 O  O   . HOH   N 6 .   ? -26.462 8.799   -18.691 1.00 34.85  ? 728 HOH   A O   1 
HETATM 2973 O  O   . HOH   N 6 .   ? -22.455 -0.534  -21.216 1.00 38.30  ? 729 HOH   A O   1 
HETATM 2974 O  O   . HOH   N 6 .   ? -20.216 14.815  2.509   1.00 46.88  ? 730 HOH   A O   1 
HETATM 2975 O  O   . HOH   N 6 .   ? -9.237  11.002  -22.676 1.00 25.77  ? 731 HOH   A O   1 
HETATM 2976 O  O   . HOH   N 6 .   ? -19.555 35.520  -22.207 1.00 48.41  ? 732 HOH   A O   1 
HETATM 2977 O  O   . HOH   N 6 .   ? 2.667   16.984  -36.383 1.00 41.84  ? 733 HOH   A O   1 
HETATM 2978 O  O   . HOH   N 6 .   ? 0.501   22.497  -30.074 1.00 32.34  ? 734 HOH   A O   1 
HETATM 2979 O  O   . HOH   N 6 .   ? -7.155  14.725  -5.101  1.00 40.30  ? 735 HOH   A O   1 
HETATM 2980 O  O   . HOH   N 6 .   ? -4.358  -4.872  -10.422 1.00 53.98  ? 736 HOH   A O   1 
HETATM 2981 O  O   . HOH   N 6 .   ? -13.440 34.348  -26.969 1.00 52.29  ? 737 HOH   A O   1 
HETATM 2982 O  O   . HOH   N 6 .   ? -14.157 34.718  3.009   1.00 52.08  ? 738 HOH   A O   1 
HETATM 2983 O  O   . HOH   N 6 .   ? -27.418 13.388  -0.948  1.00 45.65  ? 739 HOH   A O   1 
HETATM 2984 O  O   . HOH   N 6 .   ? -11.895 -16.493 -12.579 1.00 47.68  ? 740 HOH   A O   1 
HETATM 2985 O  O   . HOH   N 6 .   ? -8.764  16.404  -8.606  1.00 37.20  ? 741 HOH   A O   1 
HETATM 2986 O  O   . HOH   N 6 .   ? -0.336  26.596  -27.010 1.00 36.01  ? 742 HOH   A O   1 
HETATM 2987 O  O   . HOH   N 6 .   ? 3.055   13.848  -30.795 1.00 41.96  ? 743 HOH   A O   1 
HETATM 2988 O  O   . HOH   N 6 .   ? -11.757 12.782  -1.708  1.00 38.30  ? 744 HOH   A O   1 
HETATM 2989 O  O   . HOH   N 6 .   ? -10.970 14.894  -2.428  1.00 39.50  ? 745 HOH   A O   1 
HETATM 2990 O  O   . HOH   N 6 .   ? -11.552 35.434  -7.111  1.00 49.86  ? 746 HOH   A O   1 
HETATM 2991 O  O   . HOH   N 6 .   ? -14.455 8.361   3.539   1.00 41.85  ? 747 HOH   A O   1 
HETATM 2992 O  O   . HOH   N 6 .   ? -23.762 13.320  -28.818 1.00 60.21  ? 748 HOH   A O   1 
HETATM 2993 O  O   . HOH   N 6 .   ? 0.809   14.628  -30.328 1.00 45.69  ? 749 HOH   A O   1 
HETATM 2994 O  O   . HOH   N 6 .   ? -27.364 9.228   -0.882  1.00 43.21  ? 750 HOH   A O   1 
HETATM 2995 O  O   . HOH   N 6 .   ? 11.440  7.799   -32.804 1.00 55.29  ? 751 HOH   A O   1 
HETATM 2996 O  O   . HOH   N 6 .   ? -14.287 26.068  5.756   1.00 49.65  ? 752 HOH   A O   1 
HETATM 2997 O  O   . HOH   N 6 .   ? -9.246  -6.942  0.927   1.00 60.74  ? 753 HOH   A O   1 
HETATM 2998 O  O   . HOH   N 6 .   ? -30.448 33.266  2.981   1.00 55.44  ? 754 HOH   A O   1 
HETATM 2999 O  O   . HOH   N 6 .   ? -3.887  -2.613  -37.092 1.00 39.59  ? 755 HOH   A O   1 
HETATM 3000 O  O   . HOH   N 6 .   ? -21.595 -8.661  -17.353 1.00 46.03  ? 756 HOH   A O   1 
HETATM 3001 O  O   . HOH   N 6 .   ? -12.111 27.020  -42.574 1.00 48.55  ? 757 HOH   A O   1 
HETATM 3002 O  O   . HOH   N 6 .   ? -9.147  26.810  -4.800  1.00 42.25  ? 758 HOH   A O   1 
HETATM 3003 O  O   . HOH   N 6 .   ? -17.971 5.833   4.859   1.00 49.70  ? 759 HOH   A O   1 
HETATM 3004 O  O   . HOH   N 6 .   ? -29.139 7.669   1.513   1.00 48.86  ? 760 HOH   A O   1 
HETATM 3005 O  O   . HOH   N 6 .   ? -20.945 35.294  -23.940 1.00 42.83  ? 761 HOH   A O   1 
HETATM 3006 O  O   . HOH   N 6 .   ? -22.747 6.061   -19.066 1.00 41.35  ? 762 HOH   A O   1 
HETATM 3007 O  O   . HOH   N 6 .   ? -9.638  11.273  -2.758  1.00 44.45  ? 763 HOH   A O   1 
HETATM 3008 O  O   . HOH   N 6 .   ? -21.013 0.594   -23.405 1.00 55.47  ? 764 HOH   A O   1 
HETATM 3009 O  O   . HOH   N 6 .   ? -14.844 -1.093  -1.392  1.00 41.86  ? 765 HOH   A O   1 
HETATM 3010 O  O   . HOH   N 6 .   ? -11.533 37.156  -11.973 1.00 53.75  ? 766 HOH   A O   1 
HETATM 3011 O  O   . HOH   N 6 .   ? 13.643  8.395   -31.655 1.00 56.24  ? 767 HOH   A O   1 
HETATM 3012 O  O   . HOH   N 6 .   ? -1.273  32.637  -39.965 1.00 54.76  ? 768 HOH   A O   1 
HETATM 3013 O  O   . HOH   N 6 .   ? -30.705 13.986  -4.833  1.00 45.24  ? 769 HOH   A O   1 
HETATM 3014 O  O   . HOH   N 6 .   ? -24.001 14.314  -31.310 1.00 64.81  ? 770 HOH   A O   1 
HETATM 3015 O  O   . HOH   N 6 .   ? -1.504  -4.817  -29.618 1.00 41.13  ? 771 HOH   A O   1 
HETATM 3016 O  O   . HOH   N 6 .   ? -1.562  1.820   -29.760 1.00 37.29  ? 772 HOH   A O   1 
HETATM 3017 O  O   . HOH   N 6 .   ? -3.051  -2.652  -34.330 1.00 45.61  ? 773 HOH   A O   1 
HETATM 3018 O  O   . HOH   N 6 .   ? -7.759  12.368  -1.610  1.00 50.92  ? 774 HOH   A O   1 
HETATM 3019 O  O   . HOH   N 6 .   ? -4.917  -4.515  -32.730 1.00 42.04  ? 775 HOH   A O   1 
HETATM 3020 O  O   . HOH   N 6 .   ? -0.479  4.065   -32.978 1.00 45.24  ? 776 HOH   A O   1 
HETATM 3021 O  O   . HOH   N 6 .   ? -13.076 38.480  -12.968 1.00 55.10  ? 777 HOH   A O   1 
HETATM 3022 O  O   . HOH   N 6 .   ? -11.535 -15.127 -15.126 1.00 45.59  ? 778 HOH   A O   1 
HETATM 3023 O  O   . HOH   N 6 .   ? -17.875 8.014   5.903   1.00 51.15  ? 779 HOH   A O   1 
HETATM 3024 O  O   . HOH   N 6 .   ? -31.058 38.332  -16.721 1.00 55.61  ? 780 HOH   A O   1 
# 
